Host Interactions of HIV factors (Homo sapiens)

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7, 4619221810, 205126, 36282418324, 16, 3785237, 4711, 38421824512252381, 9522, 4923, 43, 445422511028810, 2055525152837, 4013392531, 423813, 25, 3456, 15, 29, 33, 41...7181234828nucleoplasmmitochondrial matrixGolgi lumenearly endosome membranemitochondrial intermembrane spaceendoplasmic reticulum lumencytosolearly endosome membraneAP2S1 MA (P04591) protein UBC(1-76) AAAS RanBP1:Ran-GTP:CRM1:Rev-bound mRNA complexmyristoylated NefProtein(UniProt:P04601)p6 (P04591) protein multi-ubiquitinatedAPOBEC3G:Vif:Cul5:SCF complexREV (P04618) protein RANBP1 AP1B1 SKP1 RANBP1APOBEC3GNUP62 PSME4 PSMD8 Ran:GTPXPO1 p6 (P04585) protein VIF (P69723) proteinPSIP1 XPO1 TCEB1 PSMB9 RAN PSME2 myristoylated Nef Protein (UniProt:P04601) PSMA3 Rev-multimer Rev-multimerMA (P04585) protein Fyn:Nef ComplexPSMB10 PSIP1 Rev-multimer PSMF1 HLA class I histocompatibility antigen, A-2 alpha chain NUP62 APOBEC3G NUP188 CCNT1 AP1M1 PSMA7 NUP133 UBB(153-228) Nup45 VPR (P69726) protein APOBEC3G-3 UBC(229-304) PSMD10 PSMD3 BANF1 PACS1 NUP93 NUP43 NUP54 PSMD7 KPNB1 CD4 IN (Integrase) (P04585) protein PSMC4 Rev multimer-boundHIV-1 mRNA:CRM1complexUBB(77-152) BTRC UBA52(1-76) NUP205 Rev-multimer PSMD6 VPU (P05919) protein UBC(305-380) VIF (P69723) protein PSMA2 CCNT1 AP2M1 PSMB11 AP1S1 AP1G1 NUPL1-2 NUP160 AP2M1 UBC(229-304) UBB(1-76) NPM1 VPU (P05919) GTP NUP188 Rev multimer-boundHIV-1mRNA:Crm1:Ran:GTPPiAP2S1 AP2A2(1-939) MA (P04591) protein HLA class I histocompatibility antigen, A-2 alpha chain NUP98-3 NUP37 APOBEC3G:RTC withdeaminated minussssDNA:tRNAprimer:RNA templateXPO1PSMA8 AAAS AAAS NUP62 HIV-1 mRNA RBX1 REV (P04618) protein CD247-1 RAE1 PSMB9 HIV-1 mRNABTRC Cul5-SCF complexRan-GDPPSMD2 Vif:Cul5:SCF complexVPU (P05919) protein NUP37 REV (P04618) protein PSMB7 MA (P04585) protein CUL5 NUP98-4 PSMC6 Rev-multimer UBB(1-76) NUP54 AP1M1 REV (P04618) protein NUP43 UBC(229-304) VPRP-TEFb(CyclinT1:Cdk9) complexMA (P04591) protein PSMC4 Tat:P-TEFb(CyclinT1:Cdk9) complexGTP Rev-multimer NUP155 PSMD2 minus sssDNA containing deaminated C residues Nef:class I MHCcomplex:Ap-1:PACS-1ComplexHCKGTP RAC1 NUP188 RAC1UBB(153-228) VIF (P69723) protein PSMD12 ATP6V1HNUP35 HCK TCEB1 tRNA-Lysine3 UBC(153-228) PSMA1 IN (Integrase) (P04585) protein Importin-beta:RanGTP complexAP-2 ComplexNUPL1-2 RCC1TPR CD4 AAAS AP2S1 NUP107 AP2S1 UBA52(1-76) KPNB1 Rev-multimer VIF (P69723) protein p6 (P04585) protein PSMD9 CD4 CD28 NUP155 AP2A2(1-939) AP1S2 NUP50 VPR UBC(305-380) VPU (P05919) protein NUP210 p6 (P04585) protein AP2M1 myristoylated Nef Protein (UniProt:P04601) UBC(77-152) Nup45 MA (P04591) protein HIV-1 unspliced RNARAE1 CUL5 SEH1L-2 AP-2 ComplexUBB(77-152) HLA class I histocompatibility antigen, A-2 alpha chain myristoylated Nef Protein (UniProt:P04601) PSMD5 Rev-bound HIV-1 mRNAFYNNUP205 multiubiquitinatedCD4:Vpu:beta-TrCP_1:Skp1 complexCD4 LCK CDK9 NUP98-4 IN (Integrase) (P04585) protein NPM1AP2S1 AP2A1 PSMB5 PSMB6 myristoylated Nef Protein (UniProt:P04601) IN (Integrase) (P04585) protein CUL5 p6 (P04585) protein B2M(21-119) PSMC5 PSIP1 NUP214 MA (P04591) protein viral minus strand DNA with sticky 3' end GTP VPR NPM1 RTC with minussssDNA:tRNAprimer:RNA templateviral minus strand DNA with sticky 3' end UBC(381-456) PSMD1 BANF1 HMGA1 CD8:Nef:AP-2Complex:v-ATPaseComplexmyristoylated Nef Protein (UniProt:P04601) ADP/ATP translocasemonomer (generic)GTPLCKUBB(1-76) GTP NUP88 Importin beta-1:Revmultimer complexNUPL1-2 AP1M2 NUP85 AP2M1 TPR CD4:Vpu complexNUP35 REV (P04618) protein Nuclear Pore Complex(NPC)GTP PSMD1 Ran-GTPAP2A2(1-939) REV (P04618) protein AP1M1 viral minus strand DNA with sticky 3' end REV (P04618) protein NUP210 AP1S1 HIV-1 mRNA TPR p6 (P04591) protein PSMD9 NUP35 POM121 NUP54 Vpu:beta-TrCP1:Skp1complexAP2M1 PPIA VPU (P05919) protein AP2M1 SLC25A5 CUL5 AP-2 ComplexHMGA1 NUP43 NUP160 Rev-multimerNUP214 RANGAP1PSMA4 Reverse transcriptase/ribonuclease H APOBEC3G SLC25A6 REV (P04618) protein UBC(1-76) NUP205 NUPL1-2 PSMA8 PSMB4 XPO1 p51 (RT) RAE1 UBC(153-228) GDP APOBEC3G APOBEC3G-3 UBC(457-532) UBC(381-456) NH3UBC(457-532) HMGA1 PSME3 POM121 NUP50 CD28 B2M(21-119) VIF (P69723) protein Nef:class I MHCcomplex:AP-1:PACS-1ComplexIN (Integrase) (P04585) protein NUP93 HIV-1 mRNA CD8:Nef ComplexPACS1 APOBEC3G:Vif:Cul5:SCF complexAP2A2(1-939) CD4 minus sssDNA ATP6V1H UBC(153-228) ATP6V1H PSMB3 PSMD14 NPM1 RANBP2 KPNB1 ELMO1CCNT1REV (P04618) protein RBX1 APOBEC3G VPU (P05919) PSMA1 NUP54 p6 (P04591) protein APOBEC3G ATP6V1H IN (Integrase) (P04585) protein BTRCRANBP2 CD28 UBA52(1-76) RAN B2M(21-119) RAN KPNB1CD4NUP98-3 NUP153 REV (P04618) protein CD28:Nef:Clathrin-coated Pit Adapter Protein ComplexSKP1 NUP210 AP2M1PSMC1 p51 (RT) AP2A1 NUP107 Nef:class I MHCcomplexPSMB7 APOBEC3G-3 KPNB1 DOCK2 UBC(609-684) RPS27A(1-76) ELMO1 HMGA1 NUP98-3 CD4 NUP133 AP1B1 PSMA3 AP-1 ComplexRPS27A(1-76) AP2A2(1-939) p6 (P04591) protein BTRC APOBEC3G-3 Vif:APOBEC3G complexAP2B1 LCKSEH1L-2 DOCK2POM121 AP2B1 TCEB2 class I MHC complexREV (P04618) protein NUP98-5 tRNA-Lysine3 PSMD13 VIF (P69723) protein myristoylated Nef Protein (UniProt:P04601) AP1S3 26S proteasomemyristoylated Nef Protein (UniProt:P04601) AP2A1 NUPL2 PSMD6 RPS27A(1-76) RAN XPO1NUP98-4 myristoylated Nef Protein (UniProt:P04601) PSMC5 AP1S1 NUP37 BANF1 APOBEC3G-3 TCEB2 Rev-multimer HIV-1 mRNA myristoylated Nef Protein (UniProt:P04601) CD4SLC25A5 PSMD10 AP2S1 26S proteasomePSMB1 MA (P04585) protein GDPNUP98-3 ATP6V1HRev-multimer NUP153 p6 (P04591) protein NUP98-5 viral plus strand DNA with sticky 3' end UBC(609-684) NUP153 AP1G1 RANBP2 Revmultimer-boundHIV-1mRNA:Crm1:Ran:GTP:NPCRANBP2 NUP214 NUP62 PSME2 PAK2(1-524)PSMB3 myristoylated Nef Protein (UniProt:P04601) CD4:Nef ComplexNUP107 HLA class I histocompatibility antigen, A-2 alpha chain PSME1 AP1M2 Lck:NefLipid Raft NPM1HIV-1 mRNA UBC(457-532) TCEB2 PAK2(1-524) RBX1 NUP93 KPNB1 TCEB1 ARF1VIF (P69723) protein NPM1 Ran GTPase:GDPAP1S2 AP2A2(1-939) MA (P04585) protein PSMA4 UBC(609-684) XPO1 APOBEC3G-3 PSMC6 VPU (P05919)KPNB1 PSME1 PSMB5 UBC(305-380) VPU (P05919) PSMD12 ATP6V1H GTP UbVIF (P69723) protein PSMA2 PSMA7 VPR (P69726) protein PSMD4 UBC(381-456) HIV-1 RNA template MA (P04585) protein AP2M1 VIF (P69723) protein NUPL2 CD28KPNA1 PIC anchored to theNPCPSMB8 Lipid RaftFYN CD4:Nef:AP-2Complex:v-ATPaseComplexMA (P04585) protein myristoylated Nef Protein (UniProt:P04601) PSMD11 NUP160 PSMC3 AP1G1 NUP93 MA (P04591) protein SEH1L-2 p6 (P04591) protein PSMC2 NUP98-4 PSMB2 SLC25A4 VIF (P69723) protein InternalizedCD4:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseNef:CD28 ComplexAP2A1 NUP210 CD4:Lck ComplexVPR RAN Rev multimer-boundHIV-1mRNA:Crm1:Ran:GTPIN bound to sticky3' ends of viralDNA in PICAP1S3 REV (P04618) protein Rev multimer-boundHIV-1 mRNAAP2A1 PPIA Vpr:importin-alphacomplexNUP98-5 PACS1PSMB4 AP2B1 Nup45 NUP43 VPU (P05919) AP2B1 Reverse transcriptase/ribonuclease H CD4 REV (P04618) proteinPSMB6 Nup45 NUP85 AP1B1 HIV-1 RNA template myristoylated Nef Protein (UniProt:P04601) Arf1:Nef:endosomalCD4RAN SLC25A4 myristoylated NefProtein(UniProt:P04601)BANF1 Nef:T cell Receptorzeta:Lipid Raft:Pak 2 ComplexCD28:Nef:Clathrin-coated Pit Adapter ProteinPSMF1 HIV-1 RNA template AP1S3 PSMA5 myristoylated NefProtein(UniProt:P04601)RAN ATP6V1HAP2A1 Rev-multimer RAN NUP155 NUP155 p6 (P04585) protein NUP85 UBC(533-608) LCK RAN Rev-multimer CD8B TPR NUP205 UBC(533-608) p6 (P04585) protein ATP6V1Hviral minus strand DNA with sticky 3' end PSMD14 REV (P04618) proteinPSMB10 RAN APOBEC3G PSMB8 AP2M1 PSMC3 AP1M2 VIF (P69723) protein NUP50 H2OUBC(1-76) PSME3 AP2M1 nucleoporin-associated Rev:Importin-beta:B23 complexNUP133 CD4:Vpu:beta-TrCP_1:Skp1 complexviral plus strand DNA with sticky 3' end NUPL2 NUP133 PSMC1 PSMA6 PSMC2 myristoylated Nef Protein (UniProt:P04601) Ran-GTPVPR (P69726) protein AP2A2(1-939) p6 (P04585) protein CD4 Tat (P04608) NUP88 PSMB2 PSMB11 ANT1:Vpr complexRAN RAE1 VPRmyristoylated Nef Protein (UniProt:P04601) MA (P04591) protein CD8B NUP153 BTRC PSMD8 AP2S1 APOBEC3G:RTC withminus sssDNA:tRNAprimer:RNA templateIN (Integrase) (P04585) protein GDP GTP InternalizedCD8:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPasePSMA5 Rev:importin-beta:B23:Ran-GTP complexVPU (P05919) protein NUP88 PSME4 PSIP1 SLC25A6 UBC(77-152) VPU (P05919) protein AP1S2 CD8B NUP188 AP2B1 NUP50 PSMA6 NUP160 DOCK2:ELMO1:RAC1:NefComplexHIV-1 mRNA PSMD4 VPR (P69726) protein Reverse transcriptase/ribonuclease H myristoylated Nef Protein (UniProt:P04601) UBC(533-608) Rev:Importin-beta:NPM1myristoylated Nef Protein (UniProt:P04601) B2M(21-119) p51 (RT) CD247-1CD4:Vpu:beta-TrCP_1tRNA-Lysine3 NUP37 TCEB2 PSMD11 APOBEC3G:HIV-1PICNUP214 POM121 NUP107 APOBEC3G UBB(77-152) minus sssDNA viral plus strand DNA with sticky 3' end AP2B1 RBX1 CD4 Hck-1:NefVPU (P05919) NUP85 VIF (P69723) protein GTP PPIA SEH1L-2 CDK9UBB(153-228) PSMB1 viral plus strand DNA with sticky 3' end REV (P04618) protein PSMD3 AP2A1 NUP98-5 myristoylated Nef Protein (UniProt:P04601) XPO1 p6 (P04591) protein Rev:Importin-beta:B23NUPL2 NUP88 NUP35 CDK9 Rev-multimer myristoylated Nef Protein (UniProt:P04601) MA (P04585) protein AP2B1 PSMD7 KPNA1Tat (P04608)APOBEC3G-3 TCEB1 UBC(77-152) SKP1 VPR VPU (P05919) protein PSMD5 myristoylated NefProtein(UniProt:P04601)REV (P04618) protein PSMD13 SKP1HIV-1 mRNA ARF1 303017, 35, 532130141421213021, 2721, 2721


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. View original pathway at:Reactome.

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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 proteasomeComplexR-HSA-68819 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
ADP/ATP translocase monomer (generic)ComplexR-HSA-164858 (Reactome)
ANT1:Vpr complexComplexR-HSA-180906 (Reactome)
AP-1 ComplexComplexR-HSA-167717 (Reactome)
AP-2 ComplexComplexR-HSA-167712 (Reactome)
AP1B1 ProteinQ10567 (Uniprot-TrEMBL)
AP1G1 ProteinO43747 (Uniprot-TrEMBL)
AP1M1 ProteinQ9BXS5 (Uniprot-TrEMBL)
AP1M2 ProteinQ9Y6Q5 (Uniprot-TrEMBL)
AP1S1 ProteinP61966 (Uniprot-TrEMBL)
AP1S2 ProteinP56377 (Uniprot-TrEMBL)
AP1S3 ProteinQ96PC3 (Uniprot-TrEMBL)
AP2A1 ProteinO95782 (Uniprot-TrEMBL)
AP2A2(1-939) ProteinO94973 (Uniprot-TrEMBL)
AP2B1 ProteinP63010 (Uniprot-TrEMBL)
AP2M1 ProteinQ96CW1 (Uniprot-TrEMBL)
AP2M1ProteinQ96CW1 (Uniprot-TrEMBL)
AP2S1 ProteinP53680 (Uniprot-TrEMBL)
APOBEC3G ProteinQ9HC16-1 (Uniprot-TrEMBL)
APOBEC3G-3 ProteinQ9HC16-3 (Uniprot-TrEMBL)
APOBEC3G:HIV-1PICComplexR-HSA-180618 (Reactome)
APOBEC3G:RTC with

deaminated minus sssDNA:tRNA

primer:RNA template		ComplexR-HSA-180744 (Reactome)
APOBEC3G:RTC with

minus sssDNA:tRNA

primer:RNA template		ComplexR-HSA-180616 (Reactome)
APOBEC3G:Vif:Cul5:SCF complexComplexR-HSA-180549 (Reactome)
APOBEC3GComplexR-HSA-180578 (Reactome)
ARF1 ProteinP84077 (Uniprot-TrEMBL)
ARF1ProteinP84077 (Uniprot-TrEMBL)
ATP6V1H ProteinQ9UI12 (Uniprot-TrEMBL)
ATP6V1HProteinQ9UI12 (Uniprot-TrEMBL)
Arf1:Nef:endosomal CD4ComplexR-HSA-200867 (Reactome)
B2M(21-119) ProteinP61769 (Uniprot-TrEMBL)
BANF1 ProteinO75531 (Uniprot-TrEMBL)
BTRC ProteinQ9Y297 (Uniprot-TrEMBL)
BTRCProteinQ9Y297 (Uniprot-TrEMBL)
CCNT1 ProteinO60563 (Uniprot-TrEMBL)
CCNT1ProteinO60563 (Uniprot-TrEMBL)
CD247-1 ProteinP20963-1 (Uniprot-TrEMBL)
CD247-1ProteinP20963-1 (Uniprot-TrEMBL)
CD28 ProteinP10747 (Uniprot-TrEMBL)
CD28:Nef:Clathrin-coated Pit Adapter Protein ComplexComplexR-HSA-167636 (Reactome)
CD28:Nef:Clathrin-coated Pit Adapter ProteinComplexR-HSA-167631 (Reactome)
CD28ProteinP10747 (Uniprot-TrEMBL)
CD4 ProteinP01730 (Uniprot-TrEMBL)
CD4:Lck ComplexComplexR-HSA-167529 (Reactome)
CD4:Nef ComplexComplexR-HSA-167596 (Reactome)
CD4:Nef:AP-2

Complex:v-ATPase

Complex		ComplexR-HSA-167544 (Reactome)
CD4:Vpu complexComplexR-HSA-180601 (Reactome)
CD4:Vpu:beta-TrCP_1:Skp1 complexComplexR-HSA-180592 (Reactome)
CD4:Vpu:beta-TrCP_1ComplexR-HSA-180532 (Reactome)
CD4ProteinP01730 (Uniprot-TrEMBL)
CD8:Nef ComplexComplexR-HSA-182194 (Reactome)
CD8:Nef:AP-2

Complex:v-ATPase

Complex		ComplexR-HSA-182158 (Reactome)
CD8B ProteinP10966 (Uniprot-TrEMBL)
CDK9 ProteinP50750 (Uniprot-TrEMBL)
CDK9ProteinP50750 (Uniprot-TrEMBL)
CUL5 ProteinQ93034 (Uniprot-TrEMBL)
Cul5-SCF complexComplexR-HSA-180596 (Reactome)
DOCK2 ProteinQ92608 (Uniprot-TrEMBL)
DOCK2:ELMO1:RAC1:Nef ComplexComplexR-HSA-200937 (Reactome)
DOCK2ProteinQ92608 (Uniprot-TrEMBL)
ELMO1 ProteinQ92556 (Uniprot-TrEMBL)
ELMO1ProteinQ92556 (Uniprot-TrEMBL)
FYN ProteinP06241 (Uniprot-TrEMBL)
FYNProteinP06241 (Uniprot-TrEMBL)
Fyn:Nef ComplexComplexR-HSA-200911 (Reactome)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCK ProteinP08631 (Uniprot-TrEMBL)
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:NefComplexR-HSA-200872 (Reactome)
IN (Integrase) (P04585) protein ProteinP04585 (Uniprot-TrEMBL)
IN bound to sticky

3' ends of viral

DNA in PIC		ComplexR-HSA-R-HIV-177526 (Reactome)
Importin beta-1:Rev multimer complexComplexR-HSA-180707 (Reactome)
Importin-beta:Ran GTP complexComplexR-HSA-180719 (Reactome)
Internalized CD4:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseComplexR-HSA-167554 (Reactome)
Internalized CD8:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseComplexR-HSA-182230 (Reactome)
KPNA1 ProteinP52294 (Uniprot-TrEMBL)
KPNA1ProteinP52294 (Uniprot-TrEMBL)
KPNB1 ProteinQ14974 (Uniprot-TrEMBL)
KPNB1ProteinQ14974 (Uniprot-TrEMBL)
LCK ProteinP06239 (Uniprot-TrEMBL)
LCKProteinP06239 (Uniprot-TrEMBL)
Lck:NefComplexR-HSA-R-HIV-200922 (Reactome)
Lipid Raft R-NUL-167540 (Reactome)
Lipid RaftR-NUL-167540 (Reactome)
MA (P04585) protein ProteinP04585 (Uniprot-TrEMBL)
MA (P04591) protein 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)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (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)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nef:CD28 ComplexComplexR-HSA-167629 (Reactome)
Nef:T cell Receptor

zeta:Lipid Raft:

Pak 2 Complex		ComplexR-HSA-167576 (Reactome)
Nef:class I MHC

complex:AP-1:PACS-1

Complex		ComplexR-HSA-182254 (Reactome)
Nef:class I MHC

complex:Ap-1:PACS-1

Complex		ComplexR-HSA-182373 (Reactome)
Nef:class I MHC complexComplexR-HSA-182256 (Reactome)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
P-TEFb(Cyclin T1:Cdk9) complexComplexR-HSA-167183 (Reactome)
PACS1 ProteinQ6VY07 (Uniprot-TrEMBL)
PACS1ProteinQ6VY07 (Uniprot-TrEMBL)
PAK2(1-524) ProteinQ13177 (Uniprot-TrEMBL)
PAK2(1-524)ProteinQ13177 (Uniprot-TrEMBL)
PIC anchored to the NPCComplexR-HSA-180610 (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)
PSMA7 ProteinO14818 (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)
PSMC1 ProteinP62191 (Uniprot-TrEMBL)
PSMC2 ProteinP35998 (Uniprot-TrEMBL)
PSMC3 ProteinP17980 (Uniprot-TrEMBL)
PSMC4 ProteinP43686 (Uniprot-TrEMBL)
PSMC5 ProteinP62195 (Uniprot-TrEMBL)
PSMC6 ProteinP62333 (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)
PSMD4 ProteinP55036 (Uniprot-TrEMBL)
PSMD5 ProteinQ16401 (Uniprot-TrEMBL)
PSMD6 ProteinQ15008 (Uniprot-TrEMBL)
PSMD7 ProteinP51665 (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)
PSMF1 ProteinQ92530 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RAC1 ProteinP63000 (Uniprot-TrEMBL)
RAC1ProteinP63000 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RAN ProteinP62826 (Uniprot-TrEMBL)
RANBP1 ProteinP43487 (Uniprot-TrEMBL)
RANBP1ProteinP43487 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RANGAP1ProteinP46060 (Uniprot-TrEMBL)
RBX1 ProteinP62877 (Uniprot-TrEMBL)
RCC1ProteinP18754 (Uniprot-TrEMBL)
REV (P04618) protein ProteinP04618 (Uniprot-TrEMBL)
REV (P04618) proteinProteinP04618 (Uniprot-TrEMBL)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
RTC with minus

sssDNA:tRNA

primer:RNA template		ComplexR-HSA-R-HIV-173774 (Reactome)
Ran GTPase:GDPComplexR-HSA-165549 (Reactome)
Ran-GDPComplexR-HSA-180701 (Reactome)
Ran-GTPComplexR-HSA-180738 (Reactome)
Ran:GTPComplexR-HSA-180686 (Reactome)
RanBP1:Ran-GTP:CRM1:Rev-bound mRNA complexComplexR-HSA-180718 (Reactome)
Rev

multimer-bound HIV-1

mRNA:Crm1:Ran:GTP:NPC		ComplexR-HSA-165531 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		ComplexR-HSA-165537 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		ComplexR-HSA-165552 (Reactome)
Rev multimer-bound

HIV-1 mRNA:CRM1

complex		ComplexR-HSA-180873 (Reactome)
Rev multimer-bound HIV-1 mRNAComplexR-HSA-R-HIV-165532 (Reactome)
Rev-bound HIV-1 mRNAComplexR-HSA-R-HIV-165535 (Reactome)
Rev-multimer R-HIV-165542 (Reactome)
Rev-multimer R-HIV-165543 (Reactome)
Rev-multimerR-HIV-165542 (Reactome)
Rev-multimerR-HIV-165543 (Reactome)
Rev:Importin-beta:B23ComplexR-HSA-180711 (Reactome)
Rev:Importin-beta:NPM1ComplexR-HSA-180724 (Reactome)
Rev:importin-beta:B23:Ran-GTP complexComplexR-HSA-180712 (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 (P04608) ProteinP04608 (Uniprot-TrEMBL)
Tat (P04608)ProteinP04608 (Uniprot-TrEMBL)
Tat:P-TEFb(Cyclin T1:Cdk9) complexComplexR-HSA-R-NUL-167237 (Reactome)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
UbComplexR-HSA-113595 (Reactome)
VIF (P69723) protein ProteinP69723 (Uniprot-TrEMBL)
VIF (P69723) proteinProteinP69723 (Uniprot-TrEMBL)
VPR (P69726) protein ProteinP69726 (Uniprot-TrEMBL)
VPR ProteinP69726 (Uniprot-TrEMBL)
VPRProteinP69726 (Uniprot-TrEMBL)
VPU (P05919) ProteinP05919 (Uniprot-TrEMBL)
VPU (P05919) protein ProteinP05919 (Uniprot-TrEMBL)
VPU (P05919)ProteinP05919 (Uniprot-TrEMBL)
Vif:APOBEC3G complexComplexR-HSA-180543 (Reactome)
Vif:Cul5:SCF complexComplexR-HSA-180539 (Reactome)
Vpr:importin-alpha complexComplexR-HSA-180623 (Reactome)
Vpu:beta-TrCP1:Skp1 complexComplexR-HSA-180567 (Reactome)
XPO1 ProteinO14980 (Uniprot-TrEMBL)
XPO1ProteinO14980 (Uniprot-TrEMBL)
class I MHC complexComplexR-HSA-182275 (Reactome)
minus sssDNA R-HIV-173823 (Reactome)
minus sssDNA containing deaminated C residues R-HIV-180629 (Reactome)
multi-ubiquitinated APOBEC3G:Vif:Cul5:SCF complexComplexR-HSA-180577 (Reactome)
multiubiquitinated CD4:Vpu:beta-TrCP_1:Skp1 complexComplexR-HSA-180530 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		ProteinP04601 (Uniprot-TrEMBL)
myristoylated Nef Protein (UniProt:P04601) ProteinP04601 (Uniprot-TrEMBL)
nucleoporin-associated Rev:Importin-beta:B23 complexComplexR-HSA-180720 (Reactome)
p51 (RT) ProteinP04585 (Uniprot-TrEMBL)
p6 (P04585) protein ProteinP04585 (Uniprot-TrEMBL)
p6 (P04591) protein ProteinP04591 (Uniprot-TrEMBL)
tRNA-Lysine3 R-HSA-173782 (Reactome)
viral minus strand DNA with sticky 3' end R-HIV-177533 (Reactome)
viral plus strand DNA with sticky 3' end R-HIV-177540 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
26S proteasomemim-catalysisR-HSA-180573 (Reactome)
26S proteasomemim-catalysisR-HSA-180603 (Reactome)
ADP/ATP translocase monomer (generic)R-HSA-180905 (Reactome)
ANT1:Vpr complexArrowR-HSA-180905 (Reactome)
AP-1 ComplexArrowR-HSA-182263 (Reactome)
AP-1 ComplexR-HSA-182279 (Reactome)
AP-2 ComplexArrowR-HSA-167601 (Reactome)
AP-2 ComplexArrowR-HSA-182171 (Reactome)
AP-2 ComplexR-HSA-167537 (Reactome)
AP-2 ComplexR-HSA-182186 (Reactome)
AP2M1R-HSA-167633 (Reactome)
APOBEC3G:HIV-1PICArrowR-HSA-180630 (Reactome)
APOBEC3G:RTC with

deaminated minus sssDNA:tRNA

primer:RNA template		ArrowR-HSA-180632 (Reactome)
APOBEC3G:RTC with

minus sssDNA:tRNA

primer:RNA template		ArrowR-HSA-180634 (Reactome)
APOBEC3G:RTC with

minus sssDNA:tRNA

primer:RNA template		R-HSA-180632 (Reactome)
APOBEC3G:Vif:Cul5:SCF complexArrowR-HSA-180555 (Reactome)
APOBEC3G:Vif:Cul5:SCF complexR-HSA-180540 (Reactome)
APOBEC3G:Vif:Cul5:SCF complexmim-catalysisR-HSA-180540 (Reactome)
APOBEC3GR-HSA-180602 (Reactome)
APOBEC3GR-HSA-180630 (Reactome)
APOBEC3GR-HSA-180634 (Reactome)
APOBEC3Gmim-catalysisR-HSA-180632 (Reactome)
ARF1R-HSA-200879 (Reactome)
ATP6V1HArrowR-HSA-167601 (Reactome)
ATP6V1HArrowR-HSA-182171 (Reactome)
ATP6V1HR-HSA-167537 (Reactome)
ATP6V1HR-HSA-182186 (Reactome)
Arf1:Nef:endosomal CD4ArrowR-HSA-200879 (Reactome)
BTRCR-HSA-180591 (Reactome)
CCNT1R-HSA-167235 (Reactome)
CD247-1R-HSA-164943 (Reactome)
CD28:Nef:Clathrin-coated Pit Adapter Protein ComplexArrowR-HSA-167633 (Reactome)
CD28:Nef:Clathrin-coated Pit Adapter Protein ComplexR-HSA-167637 (Reactome)
CD28:Nef:Clathrin-coated Pit Adapter ProteinArrowR-HSA-167637 (Reactome)
CD28R-HSA-167630 (Reactome)
CD4:Lck ComplexR-HSA-167566 (Reactome)
CD4:Nef ComplexArrowR-HSA-167566 (Reactome)
CD4:Nef ComplexR-HSA-167537 (Reactome)
CD4:Nef:AP-2

Complex:v-ATPase

Complex		ArrowR-HSA-167537 (Reactome)
CD4:Nef:AP-2

Complex:v-ATPase

Complex		R-HSA-167597 (Reactome)
CD4:Vpu complexArrowR-HSA-180606 (Reactome)
CD4:Vpu complexR-HSA-180591 (Reactome)
CD4:Vpu:beta-TrCP_1:Skp1 complexArrowR-HSA-180599 (Reactome)
CD4:Vpu:beta-TrCP_1:Skp1 complexR-HSA-180597 (Reactome)
CD4:Vpu:beta-TrCP_1:Skp1 complexmim-catalysisR-HSA-180597 (Reactome)
CD4:Vpu:beta-TrCP_1ArrowR-HSA-180591 (Reactome)
CD4:Vpu:beta-TrCP_1R-HSA-180599 (Reactome)
CD4R-HSA-180606 (Reactome)
CD4R-HSA-200879 (Reactome)
CD8:Nef ComplexR-HSA-182186 (Reactome)
CD8:Nef:AP-2

Complex:v-ATPase

Complex		ArrowR-HSA-182186 (Reactome)
CD8:Nef:AP-2

Complex:v-ATPase

Complex		R-HSA-182198 (Reactome)
CDK9R-HSA-167235 (Reactome)
Cul5-SCF complexR-HSA-180555 (Reactome)
DOCK2:ELMO1:RAC1:Nef ComplexArrowR-HSA-200952 (Reactome)
DOCK2R-HSA-200952 (Reactome)
ELMO1R-HSA-200952 (Reactome)
FYNR-HSA-200908 (Reactome)
Fyn:Nef ComplexArrowR-HSA-200908 (Reactome)
GDPArrowR-HSA-180687 (Reactome)
GTPR-HSA-180687 (Reactome)
H2OR-HSA-180632 (Reactome)
HCKR-HSA-200858 (Reactome)
HIV-1 mRNAR-HSA-165027 (Reactome)
HIV-1 unspliced RNAArrowR-HSA-165028 (Reactome)
Hck-1:NefArrowR-HSA-200858 (Reactome)
IN bound to sticky

3' ends of viral

DNA in PIC		R-HSA-180622 (Reactome)
IN bound to sticky

3' ends of viral

DNA in PIC		R-HSA-180627 (Reactome)
IN bound to sticky

3' ends of viral

DNA in PIC		R-HSA-180630 (Reactome)
Importin beta-1:Rev multimer complexArrowR-HSA-180709 (Reactome)
Importin beta-1:Rev multimer complexR-HSA-180725 (Reactome)
Importin-beta:Ran GTP complexArrowR-HSA-180736 (Reactome)
Internalized CD4:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseArrowR-HSA-167597 (Reactome)
Internalized CD4:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseR-HSA-167601 (Reactome)
Internalized CD8:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseArrowR-HSA-182198 (Reactome)
Internalized CD8:Nef:Clathrin-Coated Pit Adapter Protein:v-ATPaseR-HSA-182171 (Reactome)
KPNA1R-HSA-180627 (Reactome)
KPNB1R-HSA-180709 (Reactome)
LCKArrowR-HSA-167566 (Reactome)
LCKR-HSA-200954 (Reactome)
Lck:NefArrowR-HSA-200954 (Reactome)
Lipid RaftR-HSA-164943 (Reactome)
NH3ArrowR-HSA-180632 (Reactome)
NPM1ArrowR-HSA-180736 (Reactome)
NPM1R-HSA-180725 (Reactome)
Nef:CD28 ComplexArrowR-HSA-167630 (Reactome)
Nef:CD28 ComplexR-HSA-167633 (Reactome)
Nef:T cell Receptor

zeta:Lipid Raft:

Pak 2 Complex		ArrowR-HSA-164943 (Reactome)
Nef:class I MHC

complex:AP-1:PACS-1

Complex		ArrowR-HSA-182286 (Reactome)
Nef:class I MHC

complex:AP-1:PACS-1

Complex		R-HSA-182263 (Reactome)
Nef:class I MHC

complex:Ap-1:PACS-1

Complex		ArrowR-HSA-182279 (Reactome)
Nef:class I MHC

complex:Ap-1:PACS-1

Complex		R-HSA-182286 (Reactome)
Nef:class I MHC complexArrowR-HSA-182243 (Reactome)
Nef:class I MHC complexR-HSA-182279 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-165047 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-180732 (Reactome)
Nuclear Pore Complex (NPC)R-HSA-165043 (Reactome)
Nuclear Pore Complex (NPC)R-HSA-180622 (Reactome)
Nuclear Pore Complex (NPC)R-HSA-180710 (Reactome)
P-TEFb(Cyclin T1:Cdk9) complexArrowR-HSA-167235 (Reactome)
P-TEFb(Cyclin T1:Cdk9) complexR-HSA-167234 (Reactome)
PACS1ArrowR-HSA-182263 (Reactome)
PACS1R-HSA-182279 (Reactome)
PAK2(1-524)R-HSA-164943 (Reactome)
PIC anchored to the NPCArrowR-HSA-180622 (Reactome)
PiArrowR-HSA-165055 (Reactome)
R-HSA-164943 (Reactome) Nef drives the formation of lipid raft complexes.
R-HSA-165027 (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.
R-HSA-165028 (Reactome) The association of RanBp1 with RanGTP:CRM1:Rev promotes disassembly of the complex and release of the Rev:RNA cargo (Mahboobi et al. 2015).
R-HSA-165033 (Reactome) In order for Rev to function, multiple molecules must bind sequentiallly to the RRE (Malim and Cullen 1991).
R-HSA-165034 (Reactome) RanGTP binds to a preformed Rev-CRM1 complex.
R-HSA-165043 (Reactome) The Rev multimer-bound HIV-1 mRNA:Crm1:Ran:GTP complex associates with the NPC (Askjaer et al. 1998; Daugherty et al. 2010).
R-HSA-165047 (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).
R-HSA-165055 (Reactome) Ran-GAP, a Ran-specific GTPase-activating protein converts Ran-GTP to Ran-GDP, producing a Ran-GTP gradient across the nuclear membrane.
R-HSA-167234 (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).
R-HSA-167235 (Reactome) Tat associates with the Cyclin T1 subunit of the cellular kinase complex TAK/P-TEFb and recruits this complex to the TAR sequence in the HIV-1 RNA (Wei et al. 1998). This association between TAT, TAR and TAK/P-TEFb is believed to bring the catalytic subunit of TAK/P-TEFb in close proximity to Pol II where it hyperphosphorylates the CTD of Pol II .
R-HSA-167537 (Reactome) AP-2 is recruited to the newly formed Nef:CD4 complex
R-HSA-167566 (Reactome) Nef disrupts the CD4 Lck complex
R-HSA-167597 (Reactome) The Nef:CD4:AP-2 complex is internalized
R-HSA-167601 (Reactome) CD4 is degraded
R-HSA-167630 (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.
R-HSA-167633 (Reactome) Nef induces accelerated endocytosis of CD28 via clathrin-coated pits.
R-HSA-167637 (Reactome) Once Nef has induced endocytosis of CD28, CD28 containing vesicles are targeted for lysosomal degradation.
R-HSA-180540 (Reactome) APOBEC3G is multi-ubiquitinated by the Vif-Cul5-SCF complex.
R-HSA-180555 (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.
R-HSA-180573 (Reactome) Ubiquitinated CD4 is then subject to proteasome-mediated degradation.
R-HSA-180591 (Reactome) Vpu links beta-TrCP to CD4 at the ER membrane through interactions with beta-TrCP and the cytoplasmic tail of CD4.
R-HSA-180597 (Reactome) CD4 is ubiquitinated in the CD4:Vpu–h-βTrCP:Skp1 complex.
R-HSA-180599 (Reactome) The SKP1 component of the SCF complex is recruited to the Vpu:beta-TrCP:CD4 complex.
R-HSA-180602 (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.).

R-HSA-180603 (Reactome) Following multi-ubiquitination by the Vif-Cul5-SCF complex, APOBEC3G is degraded by the 26S proteasome.
R-HSA-180606 (Reactome) Vpu is expressed in the ER and associates with a membrane-proximal region in the cytoplasmic tail of CD4.
R-HSA-180622 (Reactome) Vpr binds to nucleoporins.
R-HSA-180627 (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) .
R-HSA-180630 (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.
R-HSA-180632 (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)
R-HSA-180634 (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.
R-HSA-180687 (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.
R-HSA-180709 (Reactome) The association of Rev with importin-beta is mediated by the Rev nuclear localisation signal.
R-HSA-180710 (Reactome) The Rev-importin beta-B23 complex is recruited to the nuclear pore by an interaction between importin beta and nucleoporin.
R-HSA-180725 (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.
R-HSA-180728 (Reactome) Inside the nucleus, Ran-GTP associates with importin-beta.
R-HSA-180732 (Reactome) Following the association of Rev with importin-beta, the Rev:B23:importin-beta complex is imported into the nucleus.
R-HSA-180736 (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.
R-HSA-180739 (Reactome) Upon translocation to the cytoplasm, RanBP1 associates with Ran-GTP in the Rev-CRM1-Ran-GTP complex.
R-HSA-180855 (Reactome) Vpr translocates to the mitochondria.
R-HSA-180885 (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.
R-HSA-180905 (Reactome) Vpr interacts with the PTPC component ANT1. This interaction induces mitochondrial membrane permeabilization and release of cytochrome c and apoptotic factors.
R-HSA-182171 (Reactome) Once the CD8alphabeta receptor has been internalized via endocytosis, the vesicles are targeted for lysosomal degradation.
R-HSA-182186 (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.
R-HSA-182198 (Reactome) The CD8alphabeta receptor is internalized via endocytosis.
R-HSA-182243 (Reactome) Nef disrupts the transport of major histocompatibility complex class I molecules by first binding to the the cytoplasmic side of the transmembrane complex.
R-HSA-182263 (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.
R-HSA-182279 (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.
R-HSA-182286 (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.
R-HSA-200858 (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.
R-HSA-200879 (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).
R-HSA-200908 (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.
R-HSA-200952 (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.
R-HSA-200954 (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.
RAC1R-HSA-200952 (Reactome)
RANBP1ArrowR-HSA-165028 (Reactome)
RANBP1ArrowR-HSA-165055 (Reactome)
RANBP1R-HSA-180739 (Reactome)
RANGAP1ArrowR-HSA-165055 (Reactome)
RCC1mim-catalysisR-HSA-180687 (Reactome)
REV (P04618) proteinArrowR-HSA-165028 (Reactome)
REV (P04618) proteinR-HSA-165027 (Reactome)
RTC with minus

sssDNA:tRNA

primer:RNA template		R-HSA-180634 (Reactome)
Ran GTPase:GDPArrowR-HSA-165055 (Reactome)
Ran-GDPR-HSA-180687 (Reactome)
Ran-GTPArrowR-HSA-180687 (Reactome)
Ran-GTPR-HSA-165034 (Reactome)
Ran-GTPR-HSA-180728 (Reactome)
Ran:GTPArrowR-HSA-165028 (Reactome)
Ran:GTPR-HSA-165055 (Reactome)
RanBP1:Ran-GTP:CRM1:Rev-bound mRNA complexArrowR-HSA-180739 (Reactome)
RanBP1:Ran-GTP:CRM1:Rev-bound mRNA complexR-HSA-165028 (Reactome)
Rev

multimer-bound HIV-1

mRNA:Crm1:Ran:GTP:NPC		ArrowR-HSA-165043 (Reactome)
Rev

multimer-bound HIV-1

mRNA:Crm1:Ran:GTP:NPC		R-HSA-165047 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		ArrowR-HSA-165034 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		ArrowR-HSA-165047 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		R-HSA-165043 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		R-HSA-180739 (Reactome)
Rev multimer-bound

HIV-1

mRNA:Crm1:Ran:GTP		mim-catalysisR-HSA-165055 (Reactome)
Rev multimer-bound

HIV-1 mRNA:CRM1

complex		ArrowR-HSA-180885 (Reactome)
Rev multimer-bound

HIV-1 mRNA:CRM1

complex		R-HSA-165034 (Reactome)
Rev multimer-bound HIV-1 mRNAArrowR-HSA-165033 (Reactome)
Rev multimer-bound HIV-1 mRNAR-HSA-180885 (Reactome)
Rev-bound HIV-1 mRNAArrowR-HSA-165027 (Reactome)
Rev-bound HIV-1 mRNAR-HSA-165033 (Reactome)
Rev-multimerArrowR-HSA-165028 (Reactome)
Rev-multimerArrowR-HSA-180736 (Reactome)
Rev-multimerR-HSA-165033 (Reactome)
Rev-multimerR-HSA-180709 (Reactome)
Rev:Importin-beta:B23ArrowR-HSA-180732 (Reactome)
Rev:Importin-beta:B23R-HSA-180728 (Reactome)
Rev:Importin-beta:NPM1ArrowR-HSA-180725 (Reactome)
Rev:Importin-beta:NPM1R-HSA-180710 (Reactome)
Rev:importin-beta:B23:Ran-GTP complexArrowR-HSA-180728 (Reactome)
Rev:importin-beta:B23:Ran-GTP complexR-HSA-180736 (Reactome)
SKP1R-HSA-180599 (Reactome)
Tat (P04608)R-HSA-167234 (Reactome)
Tat:P-TEFb(Cyclin T1:Cdk9) complexArrowR-HSA-167234 (Reactome)
UbArrowR-HSA-180573 (Reactome)
UbArrowR-HSA-180603 (Reactome)
UbR-HSA-180540 (Reactome)
UbR-HSA-180597 (Reactome)
VIF (P69723) proteinR-HSA-180602 (Reactome)
VPRArrowR-HSA-180855 (Reactome)
VPRR-HSA-180855 (Reactome)
VPRR-HSA-180905 (Reactome)
VPU (P05919)R-HSA-180606 (Reactome)
Vif:APOBEC3G complexArrowR-HSA-180602 (Reactome)
Vif:APOBEC3G complexR-HSA-180555 (Reactome)
Vif:APOBEC3G complexTBarR-HSA-180630 (Reactome)
Vif:Cul5:SCF complexArrowR-HSA-180603 (Reactome)
Vpr:importin-alpha complexArrowR-HSA-180627 (Reactome)
Vpu:beta-TrCP1:Skp1 complexArrowR-HSA-180573 (Reactome)
XPO1ArrowR-HSA-165028 (Reactome)
XPO1R-HSA-180885 (Reactome)
class I MHC complexR-HSA-182243 (Reactome)
multi-ubiquitinated APOBEC3G:Vif:Cul5:SCF complexArrowR-HSA-180540 (Reactome)
multi-ubiquitinated APOBEC3G:Vif:Cul5:SCF complexR-HSA-180603 (Reactome)
multiubiquitinated CD4:Vpu:beta-TrCP_1:Skp1 complexArrowR-HSA-180597 (Reactome)
multiubiquitinated CD4:Vpu:beta-TrCP_1:Skp1 complexR-HSA-180573 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		ArrowR-HSA-167601 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		ArrowR-HSA-182171 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		ArrowR-HSA-182263 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-164943 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-167566 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-167630 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-182243 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-200858 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-200879 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-200908 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-200952 (Reactome)
myristoylated Nef

Protein

(UniProt:P04601)		R-HSA-200954 (Reactome)
nucleoporin-associated Rev:Importin-beta:B23 complexArrowR-HSA-180710 (Reactome)
nucleoporin-associated Rev:Importin-beta:B23 complexR-HSA-180732 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP2684"
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