Host Interactions of HIV factors (Homo sapiens)

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326, 397, 474322471715, 21, 43383329, 443113841123, 263252414, 31, 34, 42, 45...163216, 4829, 358310, 20, 4119, 29, 40202525282225392248229, 1234308327APOBEC3G Rev-bound HIV-1 mRNA Nup107 Complex Rev multimer-bound HIV-1 mRNACrm1RanGTP RanGTP Rev-bound HIV-1 mRNA CD8NefAP-2 Complexv-ATPase Complex early endosome membraneIN bound to sticky 3' ends of viral DNA APOBEC3GRTC with minus sssDNAtRNA primerRNA template Nefclass I MHC complexAP-1PACS-1 Complex Rev multimer-bound HIV-1 mRNA Ran-GTP CD4Nef Complex Ran-GTP VifAPOBEC3G complex Rev multimer-bound HIV-1 mRNACRM1 complex RT Crm1Ran GTPaseGTP multiubiquitinated CD4Vpubeta-TrCP_1Skp1 complex AP-2 Complex Revimportin-betaB23Ran-GTP complex Nuclear Pore Complex Rev multimer-bound HIV-1 mRNACrm1RanGTPNPC CD4Nef Complex APOBEC3GRTC with deaminated minus sssDNAtRNA primerRNA template AP-1 mu Nefclass I MHC complexAp-1PACS-1 Complex RevImportin-betaNPM1 ADP/ATP translocase monomer RanBP1Ran-GTPCRM1Rev-bound mRNA complex p6 protein viral DNA with 3' sticky ends Rev multimer-bound HIV-1 mRNACRM1 complex IN bound to sticky 3' ends of viral DNA Nup107 Complex Hck-1Nef RevImportin-betaB23 AP-2 Complex FynNef Complex Importin beta-1Rev multimer complex mitochondrial matrixNefT cell Receptor zetaLipid Raft Pak 2 Complex VifAPOBEC3G complex IN bound to sticky 3' ends of viral DNA in PIC Adaptor protein complex 2 RevImportin-betaB23 RTC with minus sssDNA containing deaminated C residuestRNA primerRNA template Rev multimer-bound HIV-1 mRNA AP-1 mu CD28NefClathrin-coated Pit Adapter Protein Rev multimer-bound HIV-1 mRNACrm1RanGTP Cul5-SCF complex Internalized CD8NefClathrin-Coated Pit Adapter Proteinv-ATPase AP-2 Complex Ub Adaptor protein complex 2 viral DNA with 3' sticky ends NefCD28 Complex Arf1Nefendosomal CD4 CD4Vpu complex multi-ubiquitinated APOBEC3GVifCul5SCF complex Adaptor protein complex 2 CD4Vpubeta-TrCP_1 Nuclear Pore Complex PIC anchored to the NPC CD4Vpu complex Matrix Importin beta-1Rev multimer complex AP-2 Complex Adaptor protein complex 2 Rev multimer-bound HIV-1 mRNACrm1RanGTP Nefclass I MHC complex Rev-bound HIV-1 mRNA AP-1 mu APOBEC3GHIV-1PIC p6 protein Cul5-SCF complex Vprimportin-alpha complex p6 protein LckNef Ran-GTP p6 protein APOBEC3G Rev-bound HIV-1 mRNA P-TEFbAdaptor protein complex 2 Rev multimer-bound HIV-1 mRNA Ran-GTP AP-2 Complex Rev-bound HIV-1 mRNA Nup62 Complex ANT1Vpr complex AP-2 Complex NefCD28 Complex Ran-GTP Importin beta-1Rev multimer complex CD28NefClathrin-coated Pit Adapter Protein Complex Cul5-SCF complex minus sssDNA containing deaminated C residuesRNA templatetRNA primer AP-1 Complex IN bound to sticky 3' ends of viral DNA Adaptor protein complex 2 APOBEC3G Nuclear Pore Complex Matrix 26S proteasome RT RanGTP Matrix APOBEC3G AP-2 Complex RTC with minus sssDNAtRNA primerRNA template AP-1 sigma APOBEC3GVifCul5SCF complex Matrix Importin-betaRan GTP complex CD4Lck Complex CD8Nef Complex RanGTP CD4Vpubeta-TrCP_1Skp1 complex p6 protein Nup107 Complex Rev-bound HIV-1 mRNA class I MHC complex viral DNA with 3' sticky ends Ub Rev multimer-bound HIV-1 mRNA CD4Vpubeta-TrCP_1 CD4Vpubeta-TrCP_1 Adaptor protein complex 2 RevImportin-betaNPM1 minus sssDNARNA templatetRNA primer Vpubeta-TrCP1Skp1 complex Matrix Golgi lumenAPOBEC3G nucleoplasmminus sssDNARNA templatetRNA primer class I MHC complex RTC with minus sssDNAtRNA primerRNA template Rev multimer-bound HIV-1 mRNA Ran-GTP mitochondrial intermembrane spaceAPOBEC3GVifCul5SCF complex CD4Vpu complex Nup62 Complex early endosome membraneRev multimer-bound HIV-1 mRNA Matrix Ran GTPaseGDP class I MHC complex Importin beta-1Rev multimer complex TatP-TEFbVifAPOBEC3G complex Rev-bound HIV-1 mRNA DOCK2ELMO1RAC1Nef Complex endoplasmic reticulum lumenAP-1 sigma viral DNA with 3' sticky ends IN bound to sticky 3' ends of viral DNA in PIC IN bound to sticky 3' ends of viral DNA in PIC Rev multimer-bound HIV-1 mRNACRM1 complex p6 protein Matrix Internalized CD4NefClathrin-Coated Pit Adapter Proteinv-ATPase CD4NefAP-2 Complexv-ATPase Complex Nup62 Complex Importin beta-1Rev multimer complex CD8Nef Complex 26S proteasome Ran-GDP cytosolRev multimer-bound HIV-1 mRNACrm1RanGTP CD4Vpubeta-TrCP_1Skp1 complex p6 protein nucleoporin-associated RevImportin-betaB23 complex Cul5-SCF complex class I MHC complex IN bound to sticky 3' ends of viral DNA AP-1 sigma AP-1 Complex VifCul5SCF complex CD4Vpu complex Nup62 Complex IN bound to sticky 3' ends of viral DNA in PIC Crm1Ran GTPaseGTP APOBEC3G RT Nuclear Pore Complex Nup107 Complex AP-1 Complex P-TEFbp51 VPU NUP214 VIF AP2M1 myristoylated Nef Protein KPNB1 CD4 RevImportin-betaB23VIF myristoylated Nef Protein NUP188myristoylated Nef Protein NUP155 AP1G1 NPM1 NUP188GDP PSME4 PACS1CD28NefClathrin-coated Pit Adapter Protein ComplexB2MNUP50 Nup45 GDP PSME2 BTRC PSMC6GTPPSMB10 PSMD12 Cul5-SCF complexHLA class I histocompatibility antigen, A-2 alpha chain RANBP2 myristoylated Nef Protein Nup45 AP1M2myristoylated Nef Protein RAN REV NUP205MA CD4 NUP93 CD247-1PAK2RANBP2 APOBEC3G-3 VifAPOBEC3G complexUBA52UBCPSMD4PSMD9 GTP REV UBCNUP214 PSMF1PSMB8 PiPSMD12 PSMD2 KPNB1 UBCPOM121 Nefclass I MHC complexAP2S1 UBCAP2B1 NPM1NUP188HIV-1 mRNA HCKLipid RaftRAE1 VPU BTRCNUPL2 TCEB2 PSMB1 p6 PSMD7AP1S1 MA NUP43 MA APOBEC3G-3 AAAS MA CD4PSMD13 VIF myristoylated Nef Protein PSIP1 myristoylated Nef Protein PSMD3 PSMA3 PSMD4NUP43 AP2A2myristoylated Nef Protein NUP160 PSMC3 AP2B1 MA PSMD8 26S proteasomeAP1S3 NUP155 RAN PSMD9 RANBP2 NUP62 CD8B PSMD14 CD28 TCEB1 UBCHck-1NefNUP133 RAN Rev multimer-bound HIV-1 mRNACrm1RanGTPCD4Vpubeta-TrCP_1Skp1 complexNPM1AP1B1 REV NUP35 REV PSMB11 PSMA4 UBBREV AP2A2AP2B1 PSMB6 LCKUBCRANGAP1PSMD6Reverse transcriptase/ribonuclease H AP2S1 AP2S1 ATP6V1H MA REV AP2A1 KPNB1 PSMB7 Rev multimer-bound HIV-1 mRNAADP/ATP translocase monomer TCEB2 VPU VIF RANBP2 Reverse transcriptase/ribonuclease H AAAS VPU Ran-GTPPSMB2 PSME1 AP2M1 ARF1NUP54 NUP54 XPO1 AAAS myristoylated Nef Protein XPO1 NUP54 APOBEC3GHIV-1PICVPR myristoylated Nef Protein KPNA1 AP2A1 BTRC p6 HCKGTP myristoylated Nef Protein AP1M2NUP37 VPR AP2M1 H2ONPM1 UBCNUP205PSMC4 BANF1 myristoylated Nef Protein LckNefRAN VPR MA Rev-multimerAPOBEC3GRTC with deaminated minus sssDNAtRNA primerRNA templateAP2A2PSMC2 REV PSIP1 AP2A1 PACS1VPU UBCInternalized CD4NefClathrin-Coated Pit Adapter Proteinv-ATPaseIN AP1G1 AP2S1 PSMB4 XPO1AP1B1 B2MVPU BANF1 VIF MA SLC25A5 XPO1 NUP98-5 Importin-betaRan GTP complexNUP205p6 PSMF1DOCK2 TCEB1 NUP205DOCK2ELMO1RAC1Nef ComplexRanBP1Ran-GTPCRM1Rev-bound mRNA complexNUP93 myristoylated Nef Protein VPR Nup45 Tat NUP85 PSMD3 PSME4 AP2B1 HIV-1 mRNA HIV-1 unspliced RNAAP2A1 FYNCCNT1 CD28PACS1PSMA8 NUP62 UBCVIF RBX1 myristoylated Nef Protein CD8B NUP62 VPU GTP Rev-multimerRevimportin-betaB23Ran-GTP complexRan GTPaseGDPRAC1-1APOBEC3G-3 PSMC2 LCK p6 Nefclass I MHC complexAp-1PACS-1 ComplexATP6V1HArf1Nefendosomal CD4NUPL1-2 CDK9 p6 REV PPIA GDPPSMC1CCNT1 VPU CD4Lck ComplexCUL5 SKP1AP1B1 UBBAP1M1 NUP210 SKP1 myristoylated Nef Protein p6 SEH1L-2 NUP155 HIV-1 mRNA AP1G1 Ran-GDPVPR RAC1-1 NUP214 ELMO1KPNB1 UBBREV ELMO1 CD28NefClathrin-coated Pit Adapter ProteinAP2A2CD4 UBCPSMB9 PSMA1 SEH1L-2 GTP CUL5 NPM1 NUPL1-2 AP1M1 AP2S1 CD8B PSMA7IN CD4 AP1M2HLA class I histocompatibility antigen, A-2 alpha chain POM121 DOCK2TPR AP-1 ComplexHMGA1 CDK9 CUL5 VIF UBBCD28 Importin beta-1Rev multimer complexRPS27APSMD1 NUPL1-2 NUP93 AP2A2VIF NUPL2 PSMC4 AP1S2 PSMA3 NUP35 NUP88 VPU IN UBBPSIP1 Nup45 GTP NUP210 CD4 NUP35 p6 NUP133 ARF1ATP6V1HXPO1 NUP85 REV Internalized CD8NefClathrin-Coated Pit Adapter Proteinv-ATPasePSIP1 PSMC6NUP153 RAN RAE1 AP2S1 Rev-bound HIV-1 mRNANH3PSMA5 NUP160 VPU PSME3 PSMA7AP1M1 RAN PSMD13 CUL5 PPIA NUP155 Nuclear Pore Complex AP-2 ComplexPSMA2 TatP-TEFbPSMC5 NUP133 NUP153 TPR PSMB6 RANBP1myristoylated Nef Protein PSMB3 APOBEC3GRTC with minus sssDNAtRNA primerRNA templateRAN HIV-1 RNA template IN XPO1NUP85 NUPL1-2 UBCP-TEFbHIV-1 RNA template RAE1 TCEB1 Tat SEH1L-2 UbPOM121 NUP160 GTP HMGA1 VPU SLC25A6 PSMD8 BTRC AP2M1 AP-2 ComplexATP6V1H UBCTCEB2 PSMA1 CD4PSMA5 NUP98-5 AP1S2 MA NUP50 NUP43 HIV-1 mRNA ATP6V1H PSMB2 RAN multiubiquitinated CD4Vpubeta-TrCP_1Skp1 complexVPR class I MHC complexNUP160 myristoylated Nef Protein PSMD2 REV p6 26S proteasomeRevImportin-betaNPM1PSMB11 CD4 PSMC1BANF1 CD4Vpu complexPSMA4 PSMB1 PSMB5 RTC with minus sssDNAtRNA primerRNA templateNUP37 PIC anchored to the NPCVpubeta-TrCP1Skp1 complexAP2M1 LCKHMGA1 AP1S1 UBA52VIF APOBEC3G-3 KPNB1 VIF myristoylated Nef Protein Rev multimer-bound HIV-1 mRNACrm1RanGTPNPCVprimportin-alpha complexReverse transcriptase/ribonuclease H PSMD5 AAAS HIV-1 mRNA NUP107 CD8Nef ComplexTCEB2 MA RBX1 PSMB8 XPO1 AP2M1 NUP43 AP2S1 NUPL2 PSMB5 AP2M1HIV-1 mRNA VPR PSMD11 PSMD1 AP2A2p6 multi-ubiquitinated APOBEC3GVifCul5SCF complexREV MA GTP LCK NUP98-5 PSMC3 Rev multimer-bound HIV-1 mRNACRM1 complexNUP35 UBCCD4Nef ComplexNUP85 NUP210 POM121 HLA class I histocompatibility antigen, A-2 alpha chain NUP37 myristoylated Nef Protein myristoylated Nef Protein NUP62 NUP107 RAN VPU NUP133 CD8NefAP-2 Complexv-ATPase ComplexNPM1 SEH1L-2 PSMB3 PSMB9 NUP88 NUP88 RBX1 PSME3 NUP93 NUP88 APOBEC3G-3 VIF MA HIV-1 mRNAPPIA BTRC AP2M1 PSMD14 TCEB1 UBCNUP214 SKP1 p6 HMGA1 PSMA6 NUP54 PSMB7 AP1S3 GTP AP1S3 PSMC5 PSMD11 VPU MA myristoylated Nef Protein UBCRBX1 p51 IN FynNef ComplexVIF PSMD10 PSMA6 APOBEC3GRanGTPVPR UBCRCC1NUP98-5 PSMA8 RANBP1REV NUP107 REV Ran-GTPFYNATP6V1HAP2A1 RAE1 CD28 NUP210 BANF1 IN bound to sticky 3' ends of viral DNA in PICPSMB10 CD4 GTP nucleoporin-associated RevImportin-betaB23 complexVPR NUP107 UBCp6 NUP153 UBBANT1Vpr complexUBCIN PSMB4 p6 KPNB1KPNA1NUP37 KPNB1 HLA class I histocompatibility antigen, A-2 alpha chain PSME1 AP1S2 AP2A1 APOBEC3GVifCul5SCF complexmyristoylated Nef Protein CD4 CD247-1 REV SKP1 AP1S1 p51 VifCul5SCF complexNefT cell Receptor zetaLipid Raft Pak 2 ComplexAP2A2NUP50 CD4Vpubeta-TrCP_1AP2B1 HIV-1 RNA template RPS27AAP2M1 RAN p6 AP2A1 B2MAP-2 ComplexNefCD28 ComplexCD4 Nefclass I MHC complexAP-1PACS-1 ComplexAP2B1 TPR PAK2ATP6V1HHIV-1 mRNA NUP188PSMD6ATP6V1H PSMA2 NUPL2 Rev multimer-bound HIV-1 mRNACrm1RanGTPNUP50 IN TPR REV PSMD5 NUP153 MA SLC25A4 p6 CD4NefAP-2 Complexv-ATPase ComplexAP2B1 RAN VPR AP2M1 APOBEC3G-3 PSME2 B2MPSMD7PSMD10 135, 18, 28371336, 3737


Description

Like all viruses, HIV-1 must co-opt the host cell macromolecular transport and processing machinery. HIV-1 Vpr and Rev proteins play key roles in this co-optation. Efficient HIV-1 replication likewise requires evasion of APOBEC3G-mediated mutagenesis of reverse transcripts, a process mediated by the viral Vif protein. Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=162909

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Bibliography

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  1. Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMed Europe PMC Scholia
  2. Margottin F, Bour SP, Durand H, Selig L, Benichou S, Richard V, Thomas D, Strebel K, Benarous R.; ''A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif.''; PubMed Europe PMC Scholia
  3. Vodicka MA, Koepp DM, Silver PA, Emerman M.; ''HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection.''; PubMed Europe PMC Scholia
  4. Saksela K, Cheng G, Baltimore D.; ''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.''; PubMed Europe PMC Scholia
  5. Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L.; ''The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.''; PubMed Europe PMC Scholia
  6. Meyer BE, Malim MH.; ''The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm.''; PubMed Europe PMC Scholia
  7. Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C.; ''The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.''; PubMed Europe PMC Scholia
  8. Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J.; ''The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP.''; PubMed Europe PMC Scholia
  9. Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, Yu XF.; ''Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.''; PubMed Europe PMC Scholia
  10. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC Scholia
  11. Mahboobi SH, Javanpour AA, Mofrad MR.; ''The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.''; PubMed Europe PMC Scholia
  12. Zapp ML, Green MR.; ''Sequence-specific RNA binding by the HIV-1 Rev protein.''; PubMed Europe PMC Scholia
  13. Bischoff FR, Krebber H, Kempf T, Hermes I, Ponstingl H.; ''Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport.''; PubMed Europe PMC Scholia
  14. Roeth JF, Williams M, Kasper MR, Filzen TM, Collins KL.; ''HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail.''; PubMed Europe PMC Scholia
  15. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC Scholia
  16. Moarefi I, LaFevre-Bernt M, Sicheri F, Huse M, Lee CH, Kuriyan J, Miller WT.; ''Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement.''; PubMed Europe PMC Scholia
  17. Janardhan A, Swigut T, Hill B, Myers MP, Skowronski J.; ''HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis.''; PubMed Europe PMC Scholia
  18. Marin M, Rose KM, Kozak SL, Kabat D.; ''HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.''; PubMed Europe PMC Scholia
  19. Li K, Warner CK, Hodge JA, Minoshima S, Kudoh J, Fukuyama R, Maekawa M, Shimizu Y, Shimizu N, Wallace DC.; ''A human muscle adenine nucleotide translocator gene has four exons, is located on chromosome 4, and is differentially expressed.''; PubMed Europe PMC Scholia
  20. Kamata M, Nitahara-Kasahara Y, Miyamoto Y, Yoneda Y, Aida Y.; ''Importin-alpha promotes passage through the nuclear pore complex of human immunodeficiency virus type 1 Vpr.''; PubMed Europe PMC Scholia
  21. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed Europe PMC Scholia
  22. Kobayashi M, Takaori-Kondo A, Miyauchi Y, Iwai K, Uchiyama T.; ''Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.''; PubMed Europe PMC Scholia
  23. Popov S, Rexach M, Ratner L, Blobel G, Bukrinsky M.; ''Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex.''; PubMed Europe PMC Scholia
  24. Garcia JV, Miller AD.; ''Serine phosphorylation-independent downregulation of cell-surface CD4 by nef.''; PubMed Europe PMC Scholia
  25. Le Rouzic E, Mousnier A, Rustum C, Stutz F, Hallberg E, Dargemont C, Benichou S.; ''Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1.''; PubMed Europe PMC Scholia
  26. Renkema GH, Manninen A, Mann DA, Harris M, Saksela K.; ''Identification of the Nef-associated kinase as p21-activated kinase 2.''; PubMed Europe PMC Scholia
  27. Wei P, Garber ME, Fang SM, Fischer WH, Jones KA.; ''A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA.''; PubMed Europe PMC Scholia
  28. Daugherty MD, Liu B, Frankel AD.; ''Structural basis for cooperative RNA binding and export complex assembly by HIV Rev.''; PubMed Europe PMC Scholia
  29. Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW.; ''Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.''; PubMed Europe PMC Scholia
  30. Fritz CC, Green MR.; ''HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs.''; PubMed Europe PMC Scholia
  31. Renkema GH, Manninen A, Saksela K.; ''Human immunodeficiency virus type 1 Nef selectively associates with a catalytically active subpopulation of p21-activated kinase 2 (PAK2) independently of PAK2 binding to Nck or beta-PIX.''; PubMed Europe PMC Scholia
  32. Jacotot E, Ravagnan L, Loeffler M, Ferri KF, Vieira HL, Zamzami N, Costantini P, Druillennec S, Hoebeke J, Briand JP, Irinopoulou T, Daugas E, Susin SA, Cointe D, Xie ZH, Reed JC, Roques BP, Kroemer G.; ''The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore.''; PubMed Europe PMC Scholia
  33. Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMed Europe PMC Scholia
  34. Arora VK, Molina RP, Foster JL, Blakemore JL, Chernoff J, Fredericksen BL, Garcia JV.; ''Lentivirus Nef specifically activates Pak2.''; PubMed Europe PMC Scholia
  35. Yang X, Gold MO, Tang DN, Lewis DE, Aguilar-Cordova E, Rice AP, Herrmann CH.; ''TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines.''; PubMed Europe PMC Scholia
  36. Grzesiek S, Bax A, Clore GM, Gronenborn AM, Hu JS, Kaufman J, Palmer I, Stahl SJ, Wingfield PT.; ''The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.''; PubMed Europe PMC Scholia
  37. Wang JK, Kiyokawa E, Verdin E, Trono D.; ''The Nef protein of HIV-1 associates with rafts and primes T cells for activation.''; PubMed Europe PMC Scholia
  38. Raney A, Kuo LS, Baugh LL, Foster JL, Garcia JV.; ''Reconstitution and molecular analysis of an active human immunodeficiency virus type 1 Nef/p21-activated kinase 2 complex.''; PubMed Europe PMC Scholia
  39. Sheehy AM, Gaddis NC, Malim MH.; ''The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.''; PubMed Europe PMC Scholia
  40. Henderson BR, Percipalle P.; ''Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta.''; PubMed Europe PMC Scholia
  41. Wei BL, Arora VK, Raney A, Kuo LS, Xiao GH, O'Neill E, Testa JR, Foster JL, Garcia JV.; ''Activation of p21-activated kinase 2 by human immunodeficiency virus type 1 Nef induces merlin phosphorylation.''; PubMed Europe PMC Scholia
  42. Voges D, Zwickl P, Baumeister W.; ''The 26S proteasome: a molecular machine designed for controlled proteolysis.''; PubMed Europe PMC Scholia
  43. Bischoff FR, Ponstingl H.; ''Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1.''; PubMed Europe PMC Scholia
  44. Szebeni A, Mehrotra B, Baumann A, Adam SA, Wingfield PT, Olson MO.; ''Nucleolar protein B23 stimulates nuclear import of the HIV-1 Rev protein and NLS-conjugated albumin.''; PubMed Europe PMC Scholia
  45. Herrmann CH, Rice AP.; ''Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor.''; PubMed Europe PMC Scholia
  46. Malim MH, Tiley LS, McCarn DF, Rusche JR, Hauber J, Cullen BR.; ''HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence.''; PubMed Europe PMC Scholia
  47. Yi R, Bogerd HP, Cullen BR.; ''Recruitment of the Crm1 nuclear export factor is sufficient to induce cytoplasmic expression of incompletely spliced human immunodeficiency virus mRNAs.''; PubMed Europe PMC Scholia
  48. Fankhauser C, Izaurralde E, Adachi Y, Wingfield P, Laemmli UK.; ''Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.''; PubMed Europe PMC Scholia
  49. Malim MH, Cullen BR.; ''HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency.''; PubMed Europe PMC Scholia
  50. Fauré J, Stalder R, Borel C, Sobo K, Piguet V, Demaurex N, Gruenberg J, Trono D.; ''ARF1 regulates Nef-induced CD4 degradation.''; PubMed Europe PMC Scholia
  51. Swigut T, Shohdy N, Skowronski J.; ''Mechanism for down-regulation of CD28 by Nef.''; PubMed Europe PMC Scholia
  52. Yu Q, König R, Pillai S, Chiles K, Kearney M, Palmer S, Richman D, Coffin JM, Landau NR.; ''Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome.''; PubMed Europe PMC Scholia
  53. Stove V, Van de Walle I, Naessens E, Coene E, Stove C, Plum J, Verhasselt B.; ''Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta.''; PubMed Europe PMC Scholia
  54. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
  55. De Marcos Lousa C, Trézéguet V, Dianoux AC, Brandolin G, Lauquin GJ.; ''The human mitochondrial ADP/ATP carriers: kinetic properties and biogenesis of wild-type and mutant proteins in the yeast S. cerevisiae.''; PubMed Europe PMC Scholia
  56. Cheng H, Hoxie JP, Parks WP.; ''The conserved core of human immunodeficiency virus type 1 Nef is essential for association with Lck and for enhanced viral replication in T-lymphocytes.''; PubMed Europe PMC Scholia
  57. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC Scholia
  58. Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
  59. Zennou V, Perez-Caballero D, Göttlinger H, Bieniasz PD.; ''APOBEC3G incorporation into human immunodeficiency virus type 1 particles.''; PubMed Europe PMC Scholia
  60. Agopian K, Wei BL, Garcia JV, Gabuzda D.; ''CD4 and MHC-I downregulation are conserved in primary HIV-1 Nef alleles from brain and lymphoid tissues, but Pak2 activation is highly variable.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114683view16:15, 25 January 2021ReactomeTeamReactome version 75
113130view11:19, 2 November 2020ReactomeTeamReactome version 74
112362view15:29, 9 October 2020ReactomeTeamReactome version 73
101263view11:15, 1 November 2018ReactomeTeamreactome version 66
100801view20:43, 31 October 2018ReactomeTeamreactome version 65
100343view19:21, 31 October 2018ReactomeTeamreactome version 64
99888view16:03, 31 October 2018ReactomeTeamreactome version 63
99445view14:37, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
96358view20:11, 9 March 2018AndrewlmasonHIV down regulated
93974view13:49, 16 August 2017ReactomeTeamreactome version 61
93575view11:27, 9 August 2017ReactomeTeamreactome version 61
87139view18:51, 18 July 2016MkutmonOntology Term : 'infectious disease pathway' added !
86678view09:24, 11 July 2016ReactomeTeamreactome version 56
83092view09:57, 18 November 2015ReactomeTeamVersion54
81413view12:56, 21 August 2015ReactomeTeamVersion53
76883view08:15, 17 July 2014ReactomeTeamFixed remaining interactions
76588view11:56, 16 July 2014ReactomeTeamFixed remaining interactions
75920view09:57, 11 June 2014ReactomeTeamRe-fixing comment source
75621view10:48, 10 June 2014ReactomeTeamReactome 48 Update
74976view13:49, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74620view08:40, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
26S proteasomeComplexREACT_2353 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
ADP/ATP translocase monomer ProteinREACT_8605 (Reactome)
ANT1 Vpr complexComplexREACT_8897 (Reactome)
AP-1 ComplexComplexREACT_11249 (Reactome)
AP-2 ComplexComplexREACT_11732 (Reactome)
AP1B1 ProteinQ10567 (Uniprot-TrEMBL)
AP1G1 ProteinO43747 (Uniprot-TrEMBL)
AP1M1 ProteinQ9BXS5 (Uniprot-TrEMBL)
AP1M2ProteinQ9Y6Q5 (Uniprot-TrEMBL)
AP1S1 ProteinP61966 (Uniprot-TrEMBL)
AP1S2 ProteinP56377 (Uniprot-TrEMBL)
AP1S3 ProteinQ96PC3 (Uniprot-TrEMBL)
AP2A1 ProteinO95782 (Uniprot-TrEMBL)
AP2A2ProteinO94973 (Uniprot-TrEMBL)
AP2B1 ProteinP63010 (Uniprot-TrEMBL)
AP2M1 ProteinQ96CW1 (Uniprot-TrEMBL)
AP2M1ProteinQ96CW1 (Uniprot-TrEMBL)
AP2S1 ProteinP53680 (Uniprot-TrEMBL)
APOBEC3G HIV-1PICComplexREACT_9691 (Reactome)
APOBEC3G

RTC with deaminated minus sssDNA tRNA primer

RNA template		ComplexREACT_9785 (Reactome)
APOBEC3G

RTC with minus sssDNA tRNA primer

RNA template		ComplexREACT_9745 (Reactome)
APOBEC3G

Vif Cul5

SCF complex		ComplexREACT_9643 (Reactome)
APOBEC3G-3 ProteinQ9HC16-3 (Uniprot-TrEMBL)
APOBEC3GProteinREACT_9891 (Reactome)
ARF1ProteinP84077 (Uniprot-TrEMBL)
ATP6V1H ProteinQ9UI12 (Uniprot-TrEMBL)
ATP6V1HProteinQ9UI12 (Uniprot-TrEMBL)
Arf1

Nef

endosomal CD4		ComplexREACT_11580 (Reactome)
B2MProteinP61769 (Uniprot-TrEMBL)
BANF1 ProteinO75531 (Uniprot-TrEMBL)
BTRC ProteinQ9Y297 (Uniprot-TrEMBL)
BTRCProteinQ9Y297 (Uniprot-TrEMBL)
CCNT1 ProteinO60563 (Uniprot-TrEMBL)
CD247-1 ProteinP20963-1 (Uniprot-TrEMBL)
CD247-1ProteinP20963-1 (Uniprot-TrEMBL)
CD28

Nef

Clathrin-coated Pit Adapter Protein Complex		ComplexREACT_11677 (Reactome)
CD28

Nef

Clathrin-coated Pit Adapter Protein		ComplexREACT_11442 (Reactome)
CD28 ProteinP10747 (Uniprot-TrEMBL)
CD28ProteinP10747 (Uniprot-TrEMBL)
CD4 Lck ComplexComplexREACT_11737 (Reactome)
CD4

Nef AP-2 Complex

v-ATPase Complex		ComplexREACT_11339 (Reactome)
CD4 Nef ComplexComplexREACT_11987 (Reactome)
CD4

Vpu beta-TrCP_1

Skp1 complex		ComplexREACT_9120 (Reactome)
CD4

Vpu

beta-TrCP_1		ComplexREACT_9238 (Reactome)
CD4 Vpu complexComplexREACT_9255 (Reactome)
CD4 ProteinP01730 (Uniprot-TrEMBL)
CD4ProteinP01730 (Uniprot-TrEMBL)
CD8

Nef AP-2 Complex

v-ATPase Complex		ComplexREACT_11369 (Reactome)
CD8 Nef ComplexComplexREACT_11411 (Reactome)
CD8B ProteinP10966 (Uniprot-TrEMBL)
CDK9 ProteinP50750 (Uniprot-TrEMBL)
CUL5 ProteinQ93034 (Uniprot-TrEMBL)
Cul5-SCF complexComplexREACT_9690 (Reactome)
DOCK2

ELMO1 RAC1

Nef Complex		ComplexREACT_11827 (Reactome)
DOCK2 ProteinQ92608 (Uniprot-TrEMBL)
DOCK2ProteinQ92608 (Uniprot-TrEMBL)
ELMO1 ProteinQ92556 (Uniprot-TrEMBL)
ELMO1ProteinQ92556 (Uniprot-TrEMBL)
FYNProteinP06241 (Uniprot-TrEMBL)
Fyn Nef ComplexComplexREACT_11637 (Reactome)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCKProteinP08631 (Uniprot-TrEMBL)
HIV-1 RNA template ProteinAF033819 (EMBL)
HIV-1 mRNA ProteinAF033819 (EMBL)
HIV-1 mRNARnaAF033819 (EMBL)
HIV-1 unspliced RNARnaAF033819 (EMBL)
HLA class I histocompatibility antigen, A-2 alpha chain ProteinP01892 (Uniprot-TrEMBL)
HMGA1 ProteinP17096 (Uniprot-TrEMBL)
Hck-1 NefComplexREACT_11973 (Reactome)
IN ProteinP04585 (Uniprot-TrEMBL)
IN bound to sticky 3' ends of viral DNA in PICComplexREACT_8354 (Reactome)
Importin beta-1 Rev multimer complexComplexREACT_9841 (Reactome)
Importin-beta Ran GTP complexComplexREACT_9883 (Reactome)
Internalized CD4

Nef Clathrin-Coated Pit Adapter Protein

v-ATPase		ComplexREACT_11967 (Reactome)
Internalized CD8

Nef Clathrin-Coated Pit Adapter Protein

v-ATPase		ComplexREACT_11305 (Reactome)
KPNA1 ProteinP52294 (Uniprot-TrEMBL)
KPNA1ProteinP52294 (Uniprot-TrEMBL)
KPNB1 ProteinQ14974 (Uniprot-TrEMBL)
KPNB1ProteinQ14974 (Uniprot-TrEMBL)
LCK ProteinP06239 (Uniprot-TrEMBL)
LCKProteinP06239 (Uniprot-TrEMBL)
Lck NefComplexREACT_11930 (Reactome)
Lipid RaftREACT_11624 (Reactome)
MA ProteinP04585 (Uniprot-TrEMBL)
MA ProteinP04591 (Uniprot-TrEMBL)
NH3MetaboliteCHEBI:16134 (ChEBI)
NPM1 ProteinP06748 (Uniprot-TrEMBL)
NPM1ProteinP06748 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nef CD28 ComplexComplexREACT_11853 (Reactome)
Nef

T cell Receptor zeta Lipid Raft

Pak 2 Complex		ComplexREACT_11396 (Reactome)
Nef

class I MHC complex AP-1

PACS-1 Complex		ComplexREACT_11657 (Reactome)
Nef

class I MHC complex Ap-1

PACS-1 Complex		ComplexREACT_11308 (Reactome)
Nef class I MHC complexComplexREACT_11813 (Reactome)
Nuclear Pore Complex ComplexREACT_5542 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
P-TEFbComplexREACT_6577 (Reactome)
PACS1ProteinQ6VY07 (Uniprot-TrEMBL)
PAK2ProteinQ13177 (Uniprot-TrEMBL)
PIC anchored to the NPCComplexREACT_8912 (Reactome)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
PPIA ProteinP62937 (Uniprot-TrEMBL)
PSIP1 ProteinO75475 (Uniprot-TrEMBL)
PSMA1 ProteinP25786 (Uniprot-TrEMBL)
PSMA2 ProteinP25787 (Uniprot-TrEMBL)
PSMA3 ProteinP25788 (Uniprot-TrEMBL)
PSMA4 ProteinP25789 (Uniprot-TrEMBL)
PSMA5 ProteinP28066 (Uniprot-TrEMBL)
PSMA6 ProteinP60900 (Uniprot-TrEMBL)
PSMA7ProteinO14818 (Uniprot-TrEMBL)
PSMA8 ProteinQ8TAA3 (Uniprot-TrEMBL)
PSMB1 ProteinP20618 (Uniprot-TrEMBL)
PSMB10 ProteinP40306 (Uniprot-TrEMBL)
PSMB11 ProteinA5LHX3 (Uniprot-TrEMBL)
PSMB2 ProteinP49721 (Uniprot-TrEMBL)
PSMB3 ProteinP49720 (Uniprot-TrEMBL)
PSMB4 ProteinP28070 (Uniprot-TrEMBL)
PSMB5 ProteinP28074 (Uniprot-TrEMBL)
PSMB6 ProteinP28072 (Uniprot-TrEMBL)
PSMB7 ProteinQ99436 (Uniprot-TrEMBL)
PSMB8 ProteinP28062 (Uniprot-TrEMBL)
PSMB9 ProteinP28065 (Uniprot-TrEMBL)
PSMC1ProteinP62191 (Uniprot-TrEMBL)
PSMC2 ProteinP35998 (Uniprot-TrEMBL)
PSMC3 ProteinP17980 (Uniprot-TrEMBL)
PSMC4 ProteinP43686 (Uniprot-TrEMBL)
PSMC5 ProteinP62195 (Uniprot-TrEMBL)
PSMC6ProteinP62333 (Uniprot-TrEMBL)
PSMD1 ProteinQ99460 (Uniprot-TrEMBL)
PSMD10 ProteinO75832 (Uniprot-TrEMBL)
PSMD11 ProteinO00231 (Uniprot-TrEMBL)
PSMD12 ProteinO00232 (Uniprot-TrEMBL)
PSMD13 ProteinQ9UNM6 (Uniprot-TrEMBL)
PSMD14 ProteinO00487 (Uniprot-TrEMBL)
PSMD2 ProteinQ13200 (Uniprot-TrEMBL)
PSMD3 ProteinO43242 (Uniprot-TrEMBL)
PSMD4ProteinP55036 (Uniprot-TrEMBL)
PSMD5 ProteinQ16401 (Uniprot-TrEMBL)
PSMD6ProteinQ15008 (Uniprot-TrEMBL)
PSMD7ProteinP51665 (Uniprot-TrEMBL)
PSMD8 ProteinP48556 (Uniprot-TrEMBL)
PSMD9 ProteinO00233 (Uniprot-TrEMBL)
PSME1 ProteinQ06323 (Uniprot-TrEMBL)
PSME2 ProteinQ9UL46 (Uniprot-TrEMBL)
PSME3 ProteinP61289 (Uniprot-TrEMBL)
PSME4 ProteinQ14997 (Uniprot-TrEMBL)
PSMF1ProteinQ92530 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RAC1-1 ProteinP63000-1 (Uniprot-TrEMBL)
RAC1-1ProteinP63000-1 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RAN ProteinP62826 (Uniprot-TrEMBL)
RANBP1ProteinP43487 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RANGAP1ProteinP46060 (Uniprot-TrEMBL)
RBX1 ProteinP62877 (Uniprot-TrEMBL)
RCC1ProteinP18754 (Uniprot-TrEMBL)
REV ProteinP04618 (Uniprot-TrEMBL)
RPS27AProteinP62979 (Uniprot-TrEMBL)
RTC with minus sssDNA

tRNA primer

RNA template		ComplexREACT_9297 (Reactome)
Ran GTPComplexREACT_8632 (Reactome)
Ran GTPase GDPComplexREACT_6416 (Reactome)
Ran-GDPComplexREACT_9732 (Reactome)
Ran-GTPComplexREACT_8980 (Reactome)
RanBP1

Ran-GTP CRM1

Rev-bound mRNA complex		ComplexREACT_8366 (Reactome)
Rev

Importin-beta

B23		ComplexREACT_9742 (Reactome)
Rev

Importin-beta

NPM1		ComplexREACT_9868 (Reactome)
Rev

importin-beta B23

Ran-GTP complex		ComplexREACT_9842 (Reactome)
Rev multimer-bound HIV-1 mRNA CRM1 complexComplexREACT_8117 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran GTP

NPC		ComplexREACT_6537 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		ComplexREACT_6428 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		ComplexREACT_6601 (Reactome)
Rev multimer-bound HIV-1 mRNAComplexREACT_6517 (Reactome)
Rev-bound HIV-1 mRNAComplexREACT_6419 (Reactome)
Rev-multimerREACT_6379 (Reactome)
Rev-multimerREACT_6511 (Reactome)
Reverse transcriptase/ribonuclease H ProteinP04585 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SKP1 ProteinP63208 (Uniprot-TrEMBL)
SKP1ProteinP63208 (Uniprot-TrEMBL)
SLC25A4 ProteinP12235 (Uniprot-TrEMBL)
SLC25A5 ProteinP05141 (Uniprot-TrEMBL)
SLC25A6 ProteinP12236 (Uniprot-TrEMBL)
TCEB1 ProteinQ15369 (Uniprot-TrEMBL)
TCEB2 ProteinQ15370 (Uniprot-TrEMBL)
TPR ProteinP12270 (Uniprot-TrEMBL)
Tat P-TEFbComplexREACT_6496 (Reactome)
Tat ProteinP04608 (Uniprot-TrEMBL)
UBA52ProteinP62987 (Uniprot-TrEMBL)
UBBProteinP0CG47 (Uniprot-TrEMBL)
UBCProteinP0CG48 (Uniprot-TrEMBL)
UbProteinREACT_3316 (Reactome)
VIF ProteinP69723 (Uniprot-TrEMBL)
VPR ProteinP69726 (Uniprot-TrEMBL)
VPU ProteinP05919 (Uniprot-TrEMBL)
Vif APOBEC3G complexComplexREACT_9662 (Reactome)
Vif

Cul5

SCF complex		ComplexREACT_9902 (Reactome)
Vpr importin-alpha complexComplexREACT_8944 (Reactome)
Vpu

beta-TrCP1

Skp1 complex		ComplexREACT_9101 (Reactome)
XPO1 ProteinO14980 (Uniprot-TrEMBL)
XPO1ProteinO14980 (Uniprot-TrEMBL)
class I MHC complexComplexREACT_11465 (Reactome)
multi-ubiquitinated APOBEC3G

Vif Cul5

SCF complex		ComplexREACT_9570 (Reactome)
multiubiquitinated CD4

Vpu beta-TrCP_1

Skp1 complex		ComplexREACT_9344 (Reactome)
myristoylated Nef Protein ProteinP04601 (Uniprot-TrEMBL)
nucleoporin-associated Rev

Importin-beta

B23 complex		ComplexREACT_9793 (Reactome)
p51 ProteinP04585 (Uniprot-TrEMBL)
p6 ProteinP04585 (Uniprot-TrEMBL)
p6 ProteinP04591 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
26S proteasomeREACT_9018 (Reactome)
26S proteasomeREACT_9466 (Reactome)
ADP/ATP translocase monomer REACT_7958 (Reactome)
AP-1 ComplexArrowREACT_11147 (Reactome)
AP-1 ComplexREACT_11186 (Reactome)
AP-2 ComplexArrowREACT_11144 (Reactome)
AP-2 ComplexArrowREACT_11177 (Reactome)
AP-2 ComplexREACT_11091 (Reactome)
AP-2 ComplexREACT_11125 (Reactome)
AP2M1REACT_11122 (Reactome)
APOBEC3G

RTC with deaminated minus sssDNA tRNA primer

RNA template		ArrowREACT_9435 (Reactome)
APOBEC3G

RTC with minus sssDNA tRNA primer

RNA template		REACT_9435 (Reactome)
APOBEC3G

Vif Cul5

SCF complex		REACT_9471 (Reactome)
APOBEC3GREACT_9435 (Reactome)
APOBEC3GREACT_9444 (Reactome)
APOBEC3GREACT_9445 (Reactome)
APOBEC3GREACT_9450 (Reactome)
ARF1REACT_11227 (Reactome)
ATP6V1HArrowREACT_11144 (Reactome)
ATP6V1HArrowREACT_11177 (Reactome)
ATP6V1HREACT_11091 (Reactome)
ATP6V1HREACT_11125 (Reactome)
BTRCREACT_9009 (Reactome)
CD247-1REACT_11221 (Reactome)
CD28REACT_11194 (Reactome)
CD4 Lck ComplexREACT_11148 (Reactome)
CD4 Nef ComplexArrowREACT_11148 (Reactome)
CD4 Nef ComplexREACT_11091 (Reactome)
CD4

Vpu beta-TrCP_1

Skp1 complex		REACT_9063 (Reactome)
CD4

Vpu

beta-TrCP_1		REACT_9071 (Reactome)
CD4 Vpu complexREACT_9009 (Reactome)
CD4REACT_11227 (Reactome)
CD4REACT_9024 (Reactome)
CD8 Nef ComplexREACT_11125 (Reactome)
Cul5-SCF complexREACT_9469 (Reactome)
DOCK2REACT_11090 (Reactome)
ELMO1REACT_11090 (Reactome)
FYNREACT_11075 (Reactome)
GDPArrowREACT_9507 (Reactome)
GTPREACT_9507 (Reactome)
H2OREACT_9435 (Reactome)
HCKREACT_11224 (Reactome)
HIV-1 mRNAREACT_6161 (Reactome)
HIV-1 unspliced RNAArrowREACT_6318 (Reactome)
IN bound to sticky 3' ends of viral DNA in PICREACT_7952 (Reactome)
IN bound to sticky 3' ends of viral DNA in PICREACT_8011 (Reactome)
IN bound to sticky 3' ends of viral DNA in PICREACT_9450 (Reactome)
Importin beta-1 Rev multimer complexREACT_9511 (Reactome)
Importin-beta Ran GTP complexArrowREACT_9456 (Reactome)
KPNA1REACT_8011 (Reactome)
KPNB1REACT_9394 (Reactome)
LCKArrowREACT_11148 (Reactome)
LCKREACT_11220 (Reactome)
Lipid RaftREACT_11221 (Reactome)
NH3ArrowREACT_9435 (Reactome)
NPM1ArrowREACT_9456 (Reactome)
NPM1REACT_9511 (Reactome)
Nef CD28 ComplexREACT_11122 (Reactome)
Nef class I MHC complexREACT_11186 (Reactome)
Nuclear Pore Complex ArrowREACT_6340 (Reactome)
Nuclear Pore Complex ArrowREACT_9521 (Reactome)
Nuclear Pore Complex REACT_6337 (Reactome)
Nuclear Pore Complex REACT_7952 (Reactome)
Nuclear Pore Complex REACT_9516 (Reactome)
P-TEFbREACT_6356 (Reactome)
PACS1ArrowREACT_11147 (Reactome)
PACS1REACT_11186 (Reactome)
PAK2REACT_11221 (Reactome)
PiArrowREACT_6171 (Reactome)
RAC1-1REACT_11090 (Reactome)
RANBP1ArrowREACT_6171 (Reactome)
RANBP1ArrowREACT_6318 (Reactome)
RANBP1REACT_9478 (Reactome)
RANGAP1ArrowREACT_6171 (Reactome)
RCC1REACT_9507 (Reactome)
REACT_11069 (Reactome) The CD8alphabeta receptor is internalized via endocytosis.
REACT_11071 (Reactome) Nef disrupts the transport of major histocompatibility complex class I molecules by first binding to the the cytoplasmic side of the transmembrane complex.
REACT_11075 (Reactome) Nef has been shown to bind specifically to a subset of the Src family of kinases. Nef/Fyn interaction centers on a proline-rich motif (Pro-x-x-Pro), which is implicated in SH3 binding. This domain is partially disordered in the absence of the binding partner; when bound this motif fully adopts a left-handed polyproline type II helix conformation upon complex formation with the Fyn SH3 domain. Within this structure the arginine residue (Arg77) of Nef interacts with Asp 100 of the RT loop within the Fyn SH3 domain, and triggers a hydrogen-bond rearrangement which allows the loop to adapt to complement the Nef surface. The Arg96 residue of the Fyn SH3 domain is specifically accommodated in the same hydrophobic pocket of Nef. The Nef-Fyn complex forms in vivo and may have a crucial role in the T cell perturbating action of Nef by altering T cell receptor signaling.
REACT_11090 (Reactome) The infectious cycle of primate lentiviruses is intimately linked to interactions between cells of the immune system. Nef, a potent virulence factor, alters cellular environments to increase lentiviral replication in the host, functioning as an adaptor protein. Nef activates Rac in T cell lines and in primary T cells following infection with HIV-1 in the absence of antigenic stimuli. Nef activates Rac by binding the DOCK2-ELMO1 complex, and this interaction is linked to the abilities of Nef to inhibit chemotaxis and promote T cell activation. Nef targets a critical switch that regulates Rac GTPases downstream of chemokine- and antigen-initiated signaling pathways. This interaction enables Nef to influence multiple aspects of T cell function and thus provides an important mechanism by which Nef impacts pathogenesis by primate lentiviruses.
REACT_11091 (Reactome) AP-2 is recruited to the newly formed Nef:CD4 complex
REACT_11122 (Reactome) Nef induces accelerated endocytosis of CD28 via clathrin-coated pits.
REACT_11125 (Reactome) The presence of Nef accelerates endocytosis and lysosomal degradation of the transmembrane glycoprotein CD8. Nef facilitates a cascade of protein interactions that ultimately result in the degradation of internalized CD8 protein. The final set of protein interactions that direct Nef to the beta-subunit of the COPI coatomers are at this time unclear.
A number of sites within Nef are proposed to be required for CD8 down-regulation, the myristoylation signal and N-terminal anchor regions, the C-terminal flexible loop, and amino acid positions 57 to 58. Consistent with all reported Nef functions, the myristoylation signal was found to be essential for CD8 down-modulation. The flexible loop contains a dileucine-based internalization motif, which is flanked by acidic clusters and is involved in enhanced internalization of the Nef-CD4 complex.
REACT_11144 (Reactome) Once the CD8alphabeta receptor has been internalized via endocytosis, the vesicles are targeted for lysosomal degradation.
REACT_11147 (Reactome) Once the complex of Nef, major histocompatibility complex class I molecules, PACS-1 and AP-1 arrives at the endosome, the MHC I complex is targeted for degradation.
REACT_11148 (Reactome) Nef disrupts the CD4 Lck complex
REACT_11160 (Reactome) The Nef:CD4:AP-2 complex is internalized
REACT_11164 (Reactome) Once Nef has induced endocytosis of CD28, CD28 containing vesicles are targeted for lysosomal degradation.
REACT_11177 (Reactome) CD4 is degraded
REACT_11186 (Reactome) The complex formed by Nef and the major histocompatibility complex class I molecules creates binding sites for PACS-1 and the AP-1 complex.
REACT_11194 (Reactome) Down-regulation of CD28 receptors involves a dileucine-based motif in the second disordered loop of Nef, which connects Nef to adaptor protein (AP) complex, which is a part of cellular endocytosis machinery.
REACT_11220 (Reactome) The Nef protein of the primate lentiviruses, including human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV), is a myristylated protein associated with increased viral replication and enhanced pathogenicity. Both the potentiation of T-lymphocyte activation and the enhanced serine-phosphorylation of HIV-1 capsid by Nef correlate with increased viral replication. The Nef proteins from HIV-1 and SIV bind to Lck. The SH3 and SH2 domains of Lck are sufficient for coprecipitation with non-tyrosine-phosphorylated Nef proteins. The conserved core region of HIV-1 Nef is essential for the interaction with Lck and is also important for enhanced HIV-1 replication in T-lymphocytes. The SIV and HIV-1 Nef proteins are differentially tyrosine-phosphorylated. The kinase-active Lck tyrosine-phosphorylates SIVmac239 Nef but does not phosphorylate HIV-1 Nef.
REACT_11221 (Reactome) Nef drives the formation of lipid raft complexes.
REACT_11224 (Reactome) The protein Hck is a member of the Src family of non-receptor tyrosine kinases which is preferentially expressed in haematopoietic cells of the myeloid and B-lymphoid lineages. Src kinases are inhibited by tyrosine-phosphorylation at a carboxy-terminal site. The SH2 domains of these enzymes play an essential role in this regulation by binding to the tyrosine-phosphorylated tail. The SH2 domain of Hck regulates enzymatic activity indirectly; intramolecular interactions between the SH3 and catalytic domains appear to stabilize an inactive form of the kinase. The HIV-1 Nef protein, which is a high-affinity ligand for the Hck SH3 domain, binds to either the downregulated or activated form of Hck causing a large increase in Hck catalytic activity. The intact SH3-binding motif in Nef is crucial for Hck activation.
REACT_11227 (Reactome) The HIV Nef protein downregulates CD4 through sequential connection with clathrin-coated pits and the COP1 coatomer, resulting in accelerated endocytosis and lysosomal targeting. The small GTPase ARF1 controls the Nef-induced, COP-mediated late-endosomal targeting of CD4. Nef binds ARF1 directly and can recruit the GTPase onto endosomal membranes, leading to the eventual degradation of CD4 (Faure et al. 2004).
REACT_11229 (Reactome) The complex of Nef, major histocompatibility complex class I molecules, PACS-1 and AP-1 is transported from the trans-Golgi network to an endosome, where the MHC I complex will be degraded.
REACT_6140 (Reactome) RanGTP binds to a preformed Rev-CRM1 complex.
REACT_6161 (Reactome) Nuclear export of the unspliced and partially spliced HIV-1 transcripts requires the association of the HIV-1 Rev protein with a cis-acting RNA sequence known as the Rev Response Element (RRE) located within the env gene. The RRE forms a stem loop structure that associates with an arginine-rich RNA binding motif (ARM) within Rev.
REACT_6171 (Reactome) Ran-GAP, a Ran-specific GTPase-activating protein converts Ran-GTP to Ran-GDP, producing a Ran-GTP gradient across the nuclear membrane.
REACT_6228 (Reactome) In order for Rev to function, multiple molecules must bind sequentiallly to the RRE (Malim and Cullen 1991).
REACT_6318 (Reactome) The association of RanBp1 with RanGTP:CRM1:Rev promotes disassembly of the complex and release of the Rev:RNA cargo.
REACT_6337 (Reactome) The Rev multimer-bound HIV-1 mRNA:Crm1:Ran:GTP complex associates with the NPC.
REACT_6340 (Reactome) Crm1 is a nucleocytoplasmic transport factor that is believed to interact with nucleoporins facilitating docking of the RRE-Rev-CRM1-RanGTP complex to the nuclear pore and the translocation of the complex across the nuclear pore complex (see Cullen 1998) Crm1 has been found in complex with two such nucleoporins, CAN/Nup214 and Nup88 which have been shown to be components of the human nuclear pore complex (Fornerod et al., 1997).
REACT_6356 (Reactome) Tat associates with the Cyclin T1 subunit of P-TEFb (Cyclin T1:Cdk9) through a region of cysteine-rich and core sequences referred to as the ARM domain within Tat (Wei et al., 1998; see also Herrmann 1995). This interaction is believed to involve metal ions stabilized by cysteine residues in both proteins (Bieniasz et al., 1998; Garber et al., 1998).
REACT_7952 (Reactome)
REACT_7958 (Reactome) Vpr interacts with the PTPC component ANT1. This interaction induces mitochondrial membrane permeabilization and release of cytochrome c and apoptotic factors.
REACT_7969 (Reactome) Vpr translocates to the mitochondria.
REACT_8011 (Reactome) Vpr interacts with importin-alpha through alphaH1 and alphaH2. The interaction via alphaH1 is indispensable for the nuclear entry of Vpr (Kamata et al., 2005) .
REACT_9009 (Reactome) Vpu links beta-TrCP to CD4 at the ER membrane through interactions with beta-TrCP and the cytoplasmic tail of CD4.
REACT_9018 (Reactome) Ubiquitinated CD4 is then subject to proteasome-mediated degradation.
REACT_9024 (Reactome) Vpu is expressed in the ER and associates with a membrane-proximal region in the cytoplasmic tail of CD4.
REACT_9063 (Reactome) CD4 is ubiquitinated in the CD4:Vpu–h-βTrCP:Skp1 complex.
REACT_9071 (Reactome) The SKP1 component of the SCF complex is recruited to the Vpu:beta-TrCP:CD4 complex.
REACT_9394 (Reactome) The association of Rev with importin-beta is mediated by the Rev nuclear localisation signal.
REACT_9399 (Reactome) Inside the nucleus, Ran-GTP associates with importin-beta.
REACT_9435 (Reactome) During reverse transcription, APOBEC3G-mediated minus-strand deamination occurs within a CC dinucleotide context over the entire length of the HIV-1 genome (Yu et al., 2004).
The polypurine tract is essential for plus strand synthesis and is located at the 3’ end of the retroviral genome. HIV-1 encodes an additional central polypurine tract located in the middle of the genome which also serves as primer for plus strand synthesis.
Deamination of the minus strand continues throughout its synthesis with the frequency of deamination events increasing from the 5’ to 3’ regions. A 400bp region downstream of the central polypurine tract seems to be protected from deamination (Wurtzer et al., 2006)
REACT_9444 (Reactome) In the target cell, HIV-1-associated APOBEC3G binds to the HIV-1 reverse transcript minus strand and catalyzes the deamination of cytidines in a specific dinucleotide context (e.g., dCC). In contrast, APOBEC3F and APOBEC3B display a preference for dTC.
REACT_9445 (Reactome) The HIV-1 Vif protein associates with the DNA editing enzyme APOBEC3G Marin et al) . The binding site has not yet been mapped but emerging evidence suggest that the N-terminal lregion of Vif is essential for APOBEC3G recognition (Tian et al) .
Substitution of a single amino acid in the human APOBEC3G (Asp128Lys) abolishes binding and renders it resistant to HIV-1 Vif (Schrofelbauer et al; Bogerd et al.).

REACT_9450 (Reactome) APOBEC3G is incorporated into virus particles through its association with components of the viral RNA packaging machinery. It binds to the nucleocapsid portion of Gag (NC), a region of the polyprotein that associates with genomic RNA and functions in RNA encapsidation.
REACT_9456 (Reactome) The association of importin-beta with Ran-GTP causes the disassembly of the Rev-importin β-B23 complex releasing the Rev in the nucleus.
REACT_9466 (Reactome) Following multi-ubiquitination by the Vif-Cul5-SCF complex, APOBEC3G is degraded by the 26S proteasome.
REACT_9469 (Reactome) The interaction between Vif and the E3 ubiquitin ligase complex (Cullin5, Elongin B and Elongin C, and Rbx1) takes place through direct binding of the SOCS box motif in the viral protein Vif to the host protein Elongin C. Moreover, a conserved HCCH motif in Vif allows binding to Cullin 5.
REACT_9471 (Reactome) APOBEC3G is multi-ubiquitinated by the Vif-Cul5-SCF complex.
REACT_9478 (Reactome) Upon translocation to the cytoplasm, RanBP1 associates with Ran-GTP in the Rev-CRM1-Ran-GTP complex.
REACT_9507 (Reactome) Free, nuclear RanGTP is required for export processes out of the nucleus. RCC1 catalyses the conversion of Ran-GDP to Ran-GTP in the nucleus.
REACT_9511 (Reactome) B23 may function as a shuttle for the import of HIV Rev from the cytoplasm into the nucleus or nucleolus permitting additional rounds of export of viral RNAs.
REACT_9516 (Reactome) The Rev-importin β-B23 complex is recruited to the nuclear pore by an interaction between importin β and nucleoporin.
REACT_9521 (Reactome) Following the association of Rev with importin-beta, the Rev:B23:importin-beta complex is imported into the nucleus.
REACT_9530 (Reactome) CRM1 associates directly with Rev through the Rev nuclear export signal (NES) domain and acts as the nuclear export receptor for the Rev-RRE ribonucleoprotein complex.
REV ArrowREACT_6318 (Reactome)
REV REACT_6161 (Reactome)
RTC with minus sssDNA

tRNA primer

RNA template		REACT_9444 (Reactome)
Ran GTPArrowREACT_6318 (Reactome)
Ran GTPase GDPArrowREACT_6171 (Reactome)
Ran-GDPREACT_9507 (Reactome)
Ran-GTPArrowREACT_9507 (Reactome)
Ran-GTPREACT_6140 (Reactome)
Ran-GTPREACT_9399 (Reactome)
Rev

Importin-beta

B23		ArrowREACT_9521 (Reactome)
Rev

Importin-beta

B23		REACT_9399 (Reactome)
Rev

Importin-beta

NPM1		REACT_9516 (Reactome)
Rev multimer-bound HIV-1 mRNA CRM1 complexREACT_6140 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		ArrowREACT_6340 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		REACT_6171 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		REACT_6337 (Reactome)
Rev multimer-bound HIV-1 mRNA

Crm1 Ran

GTP		REACT_9478 (Reactome)
Rev multimer-bound HIV-1 mRNAREACT_9530 (Reactome)
Rev-bound HIV-1 mRNAREACT_6228 (Reactome)
Rev-multimerArrowREACT_6318 (Reactome)
Rev-multimerArrowREACT_9456 (Reactome)
Rev-multimerREACT_6228 (Reactome)
Rev-multimerREACT_9394 (Reactome)
SKP1REACT_9071 (Reactome)
Tat REACT_6356 (Reactome)
UbArrowREACT_9018 (Reactome)
UbArrowREACT_9466 (Reactome)
UbREACT_9063 (Reactome)
UbREACT_9471 (Reactome)
VIF REACT_9445 (Reactome)
VPR REACT_7958 (Reactome)
VPU REACT_9024 (Reactome)
Vif APOBEC3G complexREACT_9469 (Reactome)
Vif

Cul5

SCF complex		ArrowREACT_9466 (Reactome)
Vpu

beta-TrCP1

Skp1 complex		ArrowREACT_9018 (Reactome)
XPO1ArrowREACT_6318 (Reactome)
XPO1REACT_9530 (Reactome)
class I MHC complexREACT_11071 (Reactome)
myristoylated Nef Protein ArrowREACT_11144 (Reactome)
myristoylated Nef Protein ArrowREACT_11147 (Reactome)
myristoylated Nef Protein ArrowREACT_11177 (Reactome)
myristoylated Nef Protein REACT_11071 (Reactome)
myristoylated Nef Protein REACT_11075 (Reactome)
myristoylated Nef Protein REACT_11090 (Reactome)
myristoylated Nef Protein REACT_11148 (Reactome)
myristoylated Nef Protein REACT_11194 (Reactome)
myristoylated Nef Protein REACT_11220 (Reactome)
myristoylated Nef Protein REACT_11221 (Reactome)
myristoylated Nef Protein REACT_11224 (Reactome)
myristoylated Nef Protein REACT_11227 (Reactome)
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