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P03406

- NEF_HV1BR

UniProt

P03406 - NEF_HV1BR

Protein

Protein Nef

Gene

nef

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 By similarity.By similarity
    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).11 Publications
    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.By similarity

    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 protease

    GO - Molecular functioni

    1. ATPase binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. CD4 receptor binding Source: UniProtKB
    4. GTP binding Source: InterPro
    5. MHC class I protein binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. receptor binding Source: UniProtKB
    9. SH3 domain binding Source: UniProtKB
    10. thioesterase binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation by symbiont of host T-cell mediated immune response Source: UniProtKB
    3. negative regulation of CD4 biosynthetic process Source: UniProtKB
    4. pathogenesis Source: UniProtKB
    5. positive regulation of catalytic activity in other organism involved in symbiotic interaction Source: UniProtKB
    6. regulation of calcium-mediated signaling Source: UniProtKB
    7. regulation of T cell activation Source: UniProtKB
    8. suppression by virus of host adaptive immune response Source: UniProtKB-KW
    9. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Source: UniProtKB
    10. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB-KW
    11. suppression by virus of host autophagy Source: UniProtKB-KW
    12. viral life cycle Source: UniProtKB

    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

    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 BRU/LAI) (HIV-1)
    Taxonomic identifieri11686 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007692: 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 By similarity
    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
    Mutagenesisi2 – 32GG → AA: 70% loss of infectivity.
    Mutagenesisi20 – 201M → A: Amost complete loss of Nef-induced MHC-I down-regulation. 1 Publication
    Mutagenesisi20 – 201M → R: Amost complete loss of Nef-induced MHC-I down-regulation. 1 Publication
    Mutagenesisi71 – 711T → R: Increases infectivity by a factor of three. 1 Publication
    Mutagenesisi72 – 721P → A: Complete loss of binding to HCK SH3 domain and altered viral growth; when associated with P-76. No effect on Nef-induced CD4 down-regulation. 1 Publication
    Mutagenesisi75 – 751P → A: Complete loss of binding to HCK SH3 domain and altered viral growth; when associated with P-73. No effect on Nef-induced CD4 down-regulation. 1 Publication
    Mutagenesisi147 – 1471P → A: Complete loss of binding to HCK SH3 domain and altered viral growth. No effect on Nef-induced CD4 down-modulation. 1 Publication
    Mutagenesisi150 – 1501P → A: No effect. 1 Publication
    Mutagenesisi164 – 1652LL → AA: Loss of interaction with AP-2 complex.
    Mutagenesisi174 – 1752DD → AA: Loss of interaction with AP-2 complex.

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host
    Chaini2 – 206205Protein NefPRO_0000038335Add
    BLAST
    Chaini58 – 206149C-terminal core proteinPRO_0000038336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by host1 Publication

    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

    Protein-protein interaction databases

    DIPiDIP-29968N.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi81 – 9313
    Turni97 – 993
    Helixi104 – 11815
    Beta strandi130 – 1323
    Beta strandi136 – 1383
    Beta strandi143 – 1475
    Beta strandi181 – 1855
    Helixi187 – 1904
    Helixi194 – 1985
    Helixi200 – 2023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AVVX-ray3.00A58-206[»]
    1AVZX-ray3.00A/B58-206[»]
    1EFNX-ray2.50B/D54-205[»]
    4D8DX-ray2.52B/D58-204[»]
    DisProtiDP00048.
    ProteinModelPortaliP03406.
    SMRiP03406. Positions 2-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03406.

    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 internalizationBy similarityAdd
    BLAST
    Regioni62 – 654Acidic; stabilizes the interaction of NEF/MHC-I with host AP1M1; necessary for MHC-I internalization and interaction with host PACS1 and PACS2By similarity
    Regioni69 – 7810SH3-binding; interaction with Src family tyrosine kinasesBy similarity
    Regioni108 – 12417Mediates dimerization, Nef-PTE1 interaction, Nef-induced CD4 and MHC-I down-regulation and enhancement of infectivityBy 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 internalizationBy similarity
    Motifi164 – 1652Di-leucine internalization motif; necessary for CD4 internalizationBy similarity
    Motifi174 – 1752Diacidic; necessary for CD4 internalizationBy similarity

    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.By similarity
    The acidic region may play a stabilizing role in the formation of a ternary complex between Nef, the MHC-I cytoplasmic domain, and AP1M1.By similarity

    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.

    P03406-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGKWSKSSV VGWPTVRERM RRAEPAADGV GAASRDLEKH GAITSSNTAA    50
    TNAACAWLEA QEEEEVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL 100
    IHSQRRQDIL DLWIYHTQGY FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP 150
    DKVEEANKGE NTSLLHPVSL HGMDDPEREV LEWRFDSRLA FHHVARELHP 200
    EYFKNC 206
    Length:206
    Mass (Da):23,342
    Last modified:January 23, 2007 - v3
    Checksum:i77453FC80B6004F2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111V → I in strain: Clone pNL4-3.
    Natural varianti15 – 151T → A in strain: Clone pNL4-3.
    Natural varianti33 – 331A → V in strain: Clone pNL4-3.
    Natural varianti51 – 511T → N in strain: Clone pNL4-3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02013 Genomic RNA. Translation: AAB59752.1.
    M19921 Genomic RNA. Translation: AAA44993.1.
    A04321 Unassigned RNA. Translation: CAA00353.1.
    PIRiA04008. ASLJFV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02013 Genomic RNA. Translation: AAB59752.1 .
    M19921 Genomic RNA. Translation: AAA44993.1 .
    A04321 Unassigned RNA. Translation: CAA00353.1 .
    PIRi A04008. ASLJFV.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AVV X-ray 3.00 A 58-206 [» ]
    1AVZ X-ray 3.00 A/B 58-206 [» ]
    1EFN X-ray 2.50 B/D 54-205 [» ]
    4D8D X-ray 2.52 B/D 58-204 [» ]
    DisProti DP00048.
    ProteinModelPortali P03406.
    SMRi P03406. Positions 2-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29968N.

    Chemistry

    BindingDBi P03406.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03406.

    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. "Nucleotide sequence of the AIDS virus, LAV."
      Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.
      Cell 40:9-17(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.
      Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Clone pNL4-3.
    3. "Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene."
      Chowers M.Y., Spina C.A., Kwoh T.J., Fitch N.J.S., Richman D.D., Guatelli J.C.
      J. Virol. 68:2906-2914(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, FUNCTION IN VIRULENCE, MUTAGENESIS OF 2-GLY-GLY-3.
      Strain: Clone pNL4-3.
    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, DI-LEUCINE MOTIF.
    5. "Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4."
      Saksela K., Cheng G., Baltimore D.
      EMBO J. 14:484-491(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SH3-BINDING SITE, MUTAGENESIS OF PRO-72; PRO-75; PRO-147 AND PRO-150.
    6. "Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV-1) Nef protein by HIV-1 protease."
      Gaedigk-Nitschko K., Schoen A., Wachinger G., Erfle V., Kohleisen B.
      FEBS Lett. 357:275-278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY VIRAL PROTEASE.
    7. "Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity."
      Greenway A.L., Azad A., Mills J., McPhee D.A.
      J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN LCK AND HUMAN MAPK3.
    8. "Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase."
      Welker R., Kottler H., Kalbitzer H.R., Kraeusslich H.-G.
      Virology 219:228-236(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CLEAVAGE BY VIRAL PROTEASE.
      Strain: Clone pNL4-3.
    9. "Virion incorporation of human immunodeficiency virus type 1 Nef is mediated by a bipartite membrane-targeting signal: analysis of its role in enhancement of viral infectivity."
      Welker R., Harris M., Cardel B., Kraeusslich H.-G.
      J. Virol. 72:8833-8840(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, N-TERMINAL DOMAIN.
      Strain: Clone pNL4-3.
    10. "Nef-induced major histocompatibility complex class I down-regulation is functionally dissociated from its virion incorporation, enhancement of viral infectivity, and CD4 down-regulation."
      Akari H., Arold S., Fukumori T., Okazaki T., Strebel K., Adachi A.
      J. Virol. 74:2907-2912(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF MET-20.
      Strain: clone pNL-432.
    11. Cited for: FUNCTION, INTERACTION WITH HUMAN PAK2.
    12. "Mechanism for down-regulation of CD28 by Nef."
      Swigut T., Shohdy N., Skowronski J.
      EMBO J. 20:1593-1604(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    13. "HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell."
      Geleziunas R., Xu W., Takeda K., Ichijo H., Greene W.C.
      Nature 410:834-838(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HUMAN MAP3K5.
    14. "A natural variability in the proline-rich motif of Nef modulates HIV-1 replication in primary T cells."
      Fackler O.T., Wolf D., Weber H.O., Laffert B., D'Aloja P., Schuler-Thurner B., Geffin R., Saksela K., Geyer M., Peterlin B.M., Schuler G., Baur A.S.
      Curr. Biol. 11:1294-1299(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-71.
      Strain: Clone pNL4-3.
    15. "Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis."
      Greenway A.L., McPhee D.A., Allen K., Johnstone R., Holloway G., Mills J., Azad A., Sankovich S., Lambert P.
      J. Virol. 76:2692-2702(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    16. "HIV Nef-mediated major histocompatibility complex class I down-modulation is independent of Arf6 activity."
      Larsen J.E., Massol R.H., Nieland T.J.F., Kirchhausen T.
      Mol. Biol. Cell 15:323-331(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    17. "The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4."
      Michel N., Allespach I., Venzke S., Fackler O.T., Keppler O.T.
      Curr. Biol. 15:714-723(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    18. "Expression of Nef downregulates CXCR4, the major coreceptor of human immunodeficiency virus, from the surfaces of target cells and thereby enhances resistance to superinfection."
      Venzke S., Michel N., Allespach I., Fackler O.T., Keppler O.T.
      J. Virol. 80:11141-11152(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    19. "HIV-1 Nef assembles a Src family kinase-ZAP-70/Syk-PI3K cascade to downregulate cell-surface MHC-I."
      Hung C.H., Thomas L., Ruby C.E., Atkins K.M., Morris N.P., Knight Z.A., Scholz I., Barklis E., Weinberg A.D., Shokat K.M., Thomas G.
      Cell Host Microbe 1:121-133(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Clone pNL4-3.
    20. "A diacidic motif in human immunodeficiency virus type 1 Nef is a novel determinant of binding to AP-2."
      Lindwasser O.W., Smith W.J., Chaudhuri R., Yang P., Hurley J.H., Bonifacino J.S.
      J. Virol. 82:1166-1174(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DIACIDIC MOTIF, MUTAGENESIS OF 164-LEU-LEU-165 AND 174-ASP-ASP-175, INTERACTION WITH HOST AP-2 COMPLEX.
    21. "A basic patch on alpha-adaptin is required for binding of human immunodeficiency virus type 1 Nef and cooperative assembly of a CD4-Nef-AP-2 complex."
      Chaudhuri R., Mattera R., Lindwasser O.W., Robinson M.S., Bonifacino J.S.
      J. Virol. 83:2518-2530(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A CD4-NEF-AP2 COMPLEX.
      Strain: Clone pNL4-3.
    22. "HIV-1 Nef dimerization is required for Nef-mediated receptor down-regulation and viral replication."
      Poe J.A., Smithgall T.E.
      J. Mol. Biol. 394:329-342(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
      Strain: Clone pNL4-3.
    23. "Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain."
      Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J.
      Cell 85:931-942(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 54-205 IN COMPLEX WITH A SRC FAMILY SH3 DOMAIN.

    Entry informationi

    Entry nameiNEF_HV1BR
    AccessioniPrimary (citable) accession number: P03406
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The infectious clone pNL4-3 is a chimeric provirus that consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
    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

    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