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P04601

- NEF_HV1H2

UniProt

P04601 - NEF_HV1H2

Protein

Protein Nef

Gene

nef

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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      Entry version 118 (01 Oct 2014)
      Sequence version 5 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins.
    In infected CD4+ T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection).
    Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4+ cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis By similarity.By similarity
    Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad By similarity.By similarity
    Extracellular Nef protein targets CD4+ T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei20 – 201Might play a role in AP-1 recruitment to the Nef-MHC-I complex
    Sitei57 – 582Cleavage; by viral proteaseBy similarity

    GO - Molecular functioni

    1. GTP binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. entry into host cell Source: Reactome
    3. pathogenesis Source: UniProtKB-KW
    4. regulation of defense response to virus by virus Source: Reactome
    5. suppression by virus of host adaptive immune response Source: UniProtKB-KW
    6. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Source: UniProtKB-KW
    7. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB-KW
    8. suppression by virus of host autophagy Source: UniProtKB-KW
    9. uncoating of virus Source: Reactome
    10. viral life cycle Source: Reactome
    11. viral process Source: Reactome
    12. virion assembly Source: Reactome

    Keywords - Biological processi

    Apoptosis, Host-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host autophagy by virus, Inhibition of host MHC class I molecule presentation by virus, Inhibition of host MHC class II molecule presentation by virus, Viral immunoevasion, Virulence

    Enzyme and pathway databases

    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
    REACT_11139. Nef mediated downregulation of CD28 cell surface expression.
    REACT_11166. Nef Mediated CD4 Down-regulation.
    REACT_11200. Nef Mediated CD8 Down-regulation.
    REACT_6359. Budding and maturation of HIV virion.
    REACT_6361. Late Phase of HIV Life Cycle.
    REACT_6818. Assembly Of The HIV Virion.
    REACT_6903. Binding and entry of HIV virion.
    REACT_6965. Uncoating of the HIV Virion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein Nef
    Alternative name(s):
    3'ORF
    Negative factor
    Short name:
    F-protein
    Cleaved into the following chain:
    Gene namesi
    Name:nef
    OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
    Taxonomic identifieri11706 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000002241: Genome

    Subcellular locationi

    Host cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Host cytoplasmhost perinuclear region By similarity. Virion By similarity. Secreted 2 Publications
    Note: Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved By similarity.By similarity

    GO - Cellular componenti

    1. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB-KW
    4. virion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host cytoplasm, Host membrane, Membrane, Secreted, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201M → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is internalized but not sequestred in TGN. 1 Publication
    Mutagenesisi62 – 654EEEE → AAAA: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized. Reduced interaction with host PACS1 and PACS2.
    Mutagenesisi62 – 654EEEE → AAEA: About 50% loss of Nef-induced MHC-I down-regulation.
    Mutagenesisi62 – 654EEEE → AEAA: About 50% loss of Nef-induced MHC-I down-regulation.
    Mutagenesisi62 – 654EEEE → DDDD: No effect on Nef-induced MHC-I down-regulation.
    Mutagenesisi62 – 643EEE → AAA: About 50% loss of Nef-induced MHC-I down-regulation.
    Mutagenesisi62 – 632EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
    Mutagenesisi63 – 653EEE → AAA: About 50% loss of Nef-induced MHC-I down-regulation.
    Mutagenesisi63 – 642EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
    Mutagenesisi64 – 652EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
    Mutagenesisi72 – 721P → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized; when associated with A-75. 1 Publication
    Mutagenesisi75 – 751P → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized; when associated with A-72. 1 Publication
    Mutagenesisi123 – 1231D → E: Complete loss of Nef-induced MHC-I down-regulation, CD4 down-regulation, and enhancement of infectivity. Activates PAK2 twofold over wild-type levels.

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 206205Protein NefPRO_0000038365Add
    BLAST
    Chaini58 – 206149C-terminal core proteinBy similarityPRO_0000038366Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

    Post-translational modificationi

    The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles By similarity.By similarity
    Phosphorylated on serine residues, probably by host PKC.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Expressioni

    Keywords - Developmental stagei

    Early protein

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with Nef associated p21-activated kinase (PAK2); this interaction activates PAK2. Associates with the Nef-MHC-I-AP1 complex; this complex is required for MHC-I internalization. Interacts (via C-terminus) with host PI3-kinase (via C-terminus). Interacts with host PACS1; this interaction seems to be weak. Interacts with host PACS2. Interacts with host LCK and MAPK3; these interactions inhibit the kinase activity of the latters. Interacts with host ATP6V1H; this interaction may play a role in CD4 endocytosis. Associates with the CD4-Nef-AP2 complex; this complex is required for CD4 internalization. Interacts with TCR-zeta chain; this interaction up-regulates the Fas ligand (FasL) surface expression. Interacts with various cellular proteins including MAP3K5, beta-COP, HCK, and PTE1. Interacts with human GNB2L1/RACK1; this increases Nef phosphorylation by PKC By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACOT8O147345EBI-6164028,EBI-1237371From a different organism.

    Protein-protein interaction databases

    BioGridi1205545. 63 interactions.
    IntActiP04601. 8 interactions.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi81 – 9414
    Helixi104 – 11815
    Beta strandi130 – 1323
    Beta strandi136 – 1383
    Beta strandi143 – 1475
    Helixi150 – 1578
    Helixi167 – 1704
    Beta strandi172 – 1754
    Beta strandi181 – 1855
    Helixi188 – 1914
    Helixi194 – 1985
    Helixi200 – 2023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RL2X-ray2.39C73-82[»]
    4NEEX-ray2.88C/E/H/K63-203[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5756N-terminal; associates with the host plasma membraneBy similarityAdd
    BLAST
    Regioni7 – 2620Necessary for MHC-I internalizationCuratedAdd
    BLAST
    Regioni62 – 654Acidic; stabilizes the interaction of NEF/MHC-I with host AP1M1; necessary for MHC-I internalization and interaction with host PACS1 and PACS2Curated
    Regioni69 – 7810SH3-binding; interaction with Src family tyrosine kinasesBy similarity
    Regioni108 – 12417Mediates dimerization, Nef-PTE1 interactionBy similarityAdd
    BLAST
    Regioni148 – 18033Binding to ATP6V1HBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi72 – 754PxxP; stabilizes the interaction of NEF/MHC-I with host AP1M1; necessary for MHC-I internalizationCurated
    Motifi164 – 1652Di-leucine internalization motif; necessary for CD4 internalizationCurated
    Motifi174 – 1752Diacidic; necessary for CD4 internalizationCurated

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi62 – 654Poly-Glu

    Domaini

    The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to p53 By similarity.By similarity
    The SH3-binding domain constituted of PxxP motifs mediates binding to several Src family proteins thereby regulating their tyrosine kinase activity. The same motifs also mediates the association with MAPK3, PI3-kinase and TCR-zeta By similarity.By similarity
    The di-leucine internalization motif and a diacidic motif seem to be required for binding to AP-2.
    The acidic region may play a stabilizing role in the formation of a ternary complex between Nef, the MHC-I cytoplasmic domain, and AP1M1.

    Sequence similaritiesi

    Keywords - Domaini

    SH3-binding

    Family and domain databases

    Gene3Di3.30.62.10. 1 hit.
    4.10.890.10. 1 hit.
    InterProiIPR027480. HIV-1_Nef_anchor.
    IPR027481. HIV-1_Nef_core.
    IPR001558. HIV_Nef.
    [Graphical view]
    PfamiPF00469. F-protein. 1 hit.
    [Graphical view]
    SUPFAMiSSF55671. SSF55671. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P04601-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGKWSKSSV IGWPTVRERM RRAEPAADRV GAASRDLEKH GAITSSNTAA    50
    TNAACAWLEA QEEEEVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL 100
    IHSQRRQDIL DLWIYHTQGY FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP 150
    DKIEEANKGE NTSLLHPVSL HGMDDPEREV LEWRFDSRLA FHHVARELHP 200
    EYFKNC 206
    Length:206
    Mass (Da):23,469
    Last modified:February 9, 2010 - v5
    Checksum:i5A26976E95483E9C
    GO

    Sequence cautioni

    The sequence AAB50263.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.
    The sequence AAC82597.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.
    The sequence CAA26946.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291R → G in CAA26946. (PubMed:2999715)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03187 Genomic RNA. Translation: CAA26946.1. Sequence problems.
    K03455 Genomic RNA. Translation: AAB50263.1. Sequence problems.
    AF033819 Genomic RNA. Translation: AAC82597.1. Sequence problems.
    RefSeqiNP_057857.2. NC_001802.1.

    Genome annotation databases

    GeneIDi156110.

    Cross-referencesi

    Web resourcesi

    BioAfrica HIV proteomics resource

    Nef entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03187 Genomic RNA. Translation: CAA26946.1 . Sequence problems.
    K03455 Genomic RNA. Translation: AAB50263.1 . Sequence problems.
    AF033819 Genomic RNA. Translation: AAC82597.1 . Sequence problems.
    RefSeqi NP_057857.2. NC_001802.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RL2 X-ray 2.39 C 73-82 [» ]
    4NEE X-ray 2.88 C/E/H/K 63-203 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1205545. 63 interactions.
    IntActi P04601. 8 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 156110.

    Enzyme and pathway databases

    Reactomei REACT_11068. Nef and signal transduction.
    REACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
    REACT_11139. Nef mediated downregulation of CD28 cell surface expression.
    REACT_11166. Nef Mediated CD4 Down-regulation.
    REACT_11200. Nef Mediated CD8 Down-regulation.
    REACT_6359. Budding and maturation of HIV virion.
    REACT_6361. Late Phase of HIV Life Cycle.
    REACT_6818. Assembly Of The HIV Virion.
    REACT_6903. Binding and entry of HIV virion.
    REACT_6965. Uncoating of the HIV Virion.

    Family and domain databases

    Gene3Di 3.30.62.10. 1 hit.
    4.10.890.10. 1 hit.
    InterProi IPR027480. HIV-1_Nef_anchor.
    IPR027481. HIV-1_Nef_core.
    IPR001558. HIV_Nef.
    [Graphical view ]
    Pfami PF00469. F-protein. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55671. SSF55671. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Polymorphism of the 3' open reading frame of the virus associated with the acquired immune deficiency syndrome, human T-lymphotropic virus type III."
      Ratner L., Starcich B.R., Josephs S.F., Hahn B.H., Reddy E.P., Livak K.J., Petteway S.R. Jr., Pearson M.L., Haseltine W.A., Arya S.K., Wong-staal F.
      Nucleic Acids Res. 13:8219-8229(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain."
      Aiken C., Konner J., Landau N.R., Lenburg M.E., Trono D.
      Cell 76:853-864(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Isolate HXB2-R7.
    5. "Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking."
      Mangasarian A., Piguet V., Wang J.-K., Chen Y.-L., Trono D.
      J. Virol. 73:1964-1973(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Isolate HXB2-R7.
    6. "HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes."
      Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G., Trono D.
      Nat. Cell Biol. 2:163-167(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HOST PACS1, SUBCELLULAR LOCATION.
      Strain: Isolate HXB2-R7.
    7. Cited for: FUNCTION.
    8. "HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway."
      Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.-H., Thomas G.
      Cell 111:853-866(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF MET-20; 63-GLU--GLU-65; PRO-72 AND PRO-75.
      Strain: Isolate HXB2D.
    9. "HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail."
      Roeth J.F., Williams M., Kasper M.R., Filzen T.M., Collins K.L.
      J. Cell Biol. 167:903-913(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A AP1-NEF-MHC-I COMPLEX.
    10. "Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain."
      Baugh L.L., Garcia J.V., Foster J.L.
      J. Virol. 82:9657-9667(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACIDIC REGION, INTERACTION WITH HOST PACS1, MUTAGENESIS OF 62-GLU--GLU-65.
    11. "HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) down-regulation: analysis using short interfering RNA and knock-out mice."
      Atkins K.M., Thomas L., Youker R.T., Harriff M.J., Pissani F., You H., Thomas G.
      J. Biol. Chem. 283:11772-11784(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST PACS2, INTERACTION WITH HOST PACS1, MUTAGENESIS OF 62-GLU--GLU-65.
    12. "The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail."
      Wonderlich E.R., Williams M., Collins K.L.
      J. Biol. Chem. 283:3011-3022(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
    13. "Human immunodeficiency virus type 1 Nef incorporation into virions does not increase infectivity."
      Laguette N., Benichou S., Basmaciogullari S.
      J. Virol. 83:1093-1104(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY VIRAL PROTEASE.
    14. "HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4(+) T cells."
      Lenassi M., Cagney G., Liao M., Vaupotic T., Bartholomeeusen K., Cheng Y., Krogan N.J., Plemenitas A., Peterlin B.M.
      Traffic 11:110-122(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "An MHC-I cytoplasmic domain/HIV-1 Nef fusion protein binds directly to the mu subunit of the AP-1 endosomal coat complex."
      Singh R.K., Lau D., Noviello C.M., Ghosh P., Guatelli J.C.
      PLoS ONE 4:E8364-E8364(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.

    Entry informationi

    Entry nameiNEF_HV1H2
    AccessioniPrimary (citable) accession number: P04601
    Secondary accession number(s): O09780, Q85587
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 118 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    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).

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3