Human protein: F-box/WD repeat-containing protein 1A isoform 2
Human protein sequence: MDPAEAVLQEKALKFMNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR

HIV protein: Vpu
Interaction type: competes with
Description: HIV-1 Vpu interferes with beta-TrCP to inhibit TNF-alpha-induced activation of NFkappaB
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: inhibits
Description: HIV-1 Vpu is a strong competitive inhibitor of beta-TrCP and impairs the degradation of SCF-beta-TrCP substrates such as IKBalpha, ATF4 and beta-catenin
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: Interaction of HIV-1 Vpu with betaTrCP is required for Vpu ubiquitination and degradation by the proteasome. Amino acid substitutions at serine's 52 and 56 of Vpu abolish the interaction with betaTrCP
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: HIV-1 Vpu S61A mutant efficiently interacts with endogenous betaTrCP and strongly stabilizes beta-catenin
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: HIV-1 Vpu stabilizes cellular Cdc25A and differentially affects betaTrCP-mediated degradation events at different phases of the cell cycle
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: Poly-ubiquitination of the CD4 cytosolic tail by SCFbeta-TrCP is required for HIV-1 Vpu-induced CD4 degradation
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: HIV-1 Vpu interacts with BST-2 in the trans-Golgi network or in early endosomes, leading to lysosomal degradation of BST-2. Vpu-mediated downregulation of BST-2 depends on cellular ubiquitination machinery via betaTrCP
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: HIV-1 Vpu and beta-TrCP co-immunoprecipitate with tetherin
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: The invariant leucine 63 and the valine 68 within the predicted second alpha-helical domain of the HIV-1 Vpu cytoplasmic tail are required for CD4 down-modulation. L63A and V68A mutants still bind CD4 and retain the ability to interact with beta-TrCP1
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: Co-depletion of beta-TrCP1 and beta-TrCP2 support Vpu's activity to enhance virus release and to downregulate endogenous tetherin in TZM-bl cells
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: inhibits
Description: HIV-1 Vpu expression leads to stabilization and upregulation of p53 via inhibiting association of p53 with beta-TrCP and its subsequent ubiquitination
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: binds
Description: Most HIV-1 Vpu proteins from Cameroonian group N viruses are unable to bind beta-TrCP because of lack of a functional beta-TrCP binding site DSGxxS in Vpu
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: binds
Description: Chimeras between the TMD of HIV-1 M Vpu and the cytoplasmic domains of SIVcpzPtt, SIVcpzPts, and SIVgor Vpu proteins are capable of binding to human beta-TrCP
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: interacts with
Description: HIV-1 Vpu-induced cleavage of IRF3 is largely dependent on the ability of Vpu to interact with beta-TrCP, and mutation of the Vpu phosphorylation sites Ser52 and Ser56 greatly decreases the function of Vpu-induced IRF3 cleavage
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: requires
Description: Vpu requires BTRC to degrade BST2 (tetherin) but does not require BTRC for Vpu-mediated BST2 (tetherin) antagonism
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: binds
Description: Through binding to beta-TrCP, HIV-1 Vpu targets CD4 for degradation in the endoplasmic reticulum and also inhibits IkappaB-alpha degradation as well as NF-kappaB activation
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL

HIV protein: Vpu
Interaction type: recruits
Description: Binding of HIV-1 Vpu to beta-TrCP requires two phosphoserine residues on Vpu (amino acids 52 and 56) and results in recruitment of beta-TrCP to cellular membranes
HIV protein sequence: MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL