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BST2 bone marrow stromal cell antigen 2 [ Homo sapiens (human) ]

Gene ID: 684, updated on 3-Nov-2024

Summary

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Official Symbol: BST2provided by HGNC
Official Full Name: bone marrow stromal cell antigen 2provided by HGNC
Primary source: HGNC:HGNC:1119
See related: Ensembl:ENSG00000130303 MIM:600534; AllianceGenome:HGNC:1119
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CD317; HM1.24; TETHERIN
Summary: Bone marrow stromal cells are involved in the growth and development of B-cells. The specific function of the protein encoded by the bone marrow stromal cell antigen 2 is undetermined; however, this protein may play a role in pre-B-cell growth and in rheumatoid arthritis. [provided by RefSeq, Jul 2008]
Expression: Broad expression in ovary (RPKM 235.4), adrenal (RPKM 135.4) and 22 other tissues See more
Orthologs: mouse all
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Genomic context

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See BST2 in Genome Data Viewer

Location:: 19p13.11

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (17402939..17405630, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (17537665..17540365, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (17513748..17516439, complement)

Chromosome 19 - NC_000019.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Neuronal BST2: A Pruritic Mediator alongside Protease-Activated Receptor 2 in the IL-27-Driven Itch Pathway.
Title: Neuronal BST2: A Pruritic Mediator alongside Protease-Activated Receptor 2 in the IL-27-Driven Itch Pathway.
Autophagy-related protein 5 (ATG5) interacts with bone marrow stromal cell antigen 2 (BST2) to stimulate HBV replication through antagonizing the antiviral activity of BST2.
Title: Autophagy-related protein 5 (ATG5) interacts with bone marrow stromal cell antigen 2 (BST2) to stimulate HBV replication through antagonizing the antiviral activity of BST2.
BST2 promotes gastric cancer metastasis under the regulation of HOXD9 and PABPC1.
Title: BST2 promotes gastric cancer metastasis under the regulation of HOXD9 and PABPC1.
Tetherin Restricts SARS-CoV-2 despite the Presence of Multiple Viral Antagonists.
Title: Tetherin Restricts SARS-CoV-2 despite the Presence of Multiple Viral Antagonists.
Tetherin antagonism by SARS-CoV-2 ORF3a and spike protein enhances virus release.
Title: Tetherin antagonism by SARS-CoV-2 ORF3a and spike protein enhances virus release.
Human BST2 inhibits rabies virus release independently of cysteine-linked dimerization and asparagine-linked glycosylation.
Title: Human BST2 inhibits rabies virus release independently of cysteine-linked dimerization and asparagine-linked glycosylation.
Understanding how transmembrane domains regulate interactions between human BST-2 and the SARS-CoV-2 accessory protein ORF7a.
Title: Understanding how transmembrane domains regulate interactions between human BST-2 and the SARS-CoV-2 accessory protein ORF7a.
CD317 maintains proteostasis and cell survival in response to proteasome inhibitors by targeting calnexin for RACK1-mediated autophagic degradation.
Title: CD317 maintains proteostasis and cell survival in response to proteasome inhibitors by targeting calnexin for RACK1-mediated autophagic degradation.
ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.
Title: ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.
BST2 regulated by the transcription factor STAT1 can promote metastasis, invasion and proliferation of oral squamous cell carcinoma via the AKT/ERK1/2 signaling pathway.
Title: BST2 regulated by the transcription factor STAT1 can promote metastasis, invasion and proliferation of oral squamous cell carcinoma via the AKT/ERK1/2 signaling pathway.

Submit: New GeneRIF Correction See all GeneRIFs (244)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Capsid expressing (p24+) cells from pleural fluid of HIV-1/TB coinfected patients or in vitro infected PBMC (whit HIV-1 NL4-3 or NLAD8) downregulate HLA-A/B/C and BST2 (Tetherin) concomitantly with CD4 downregulation	PubMed
HIV-1 infectivity/virus release from cells correlates negatively with cell surface BST2 expression levels	PubMed
HIV-1 infection (VSV-G pseudotyped) of CEMT4 T cells downregulates plasma membrane expression of BST2	PubMed
Knockdown of BST-2 by siRNA enhances production of infectious HIV-1 particles in HeLa cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp160, precursor	env	HIV-1 Vpu disrupts the co-localization between HIV-1 Env and tetherin in HeLa P4-R5 cells	PubMed
	env	BST-2 co-localizes with HIV-1 Env at the virological synapse on infected T cells	PubMed
Nef	nef	HIV-1 group M Nef downregulates tetherin from the cell surface and is dependent upon amino acids at positions 4, 5, 28, 33, 40, 90, 103, and 109 in Nef	PubMed
	nef	HIV-1 (SF2) Nef downregulates BST2 (CD317/Tetherin); downregulation is dependent upon a proline-rich SH3 binding domain in Nef	PubMed
	nef	HIV-1 C1 Nef binds to residues in the N-terminus of human BST-2 (tetherin) and allows for HIV-1 release	PubMed
	nef	HIV-1 group M and O Nefs downregulate the longer isoform of human tetherin but not the shorter isoform	PubMed
	nef	Mutation of the four residues (K186V, Q188R, S192A, and L195T) in HIV-1 group O Nefs significantly reduces Nef-mediated downregulation of human tetherin	PubMed
	nef	HIV-1 group O Nefs evolve the ability to downregulate surface levels of tetherin and sequester it to intracellular perinuclear compartments	PubMed
	nef	Residues I163 and C169 of HIV-1 Nef from chimpanzee-adapted HIV-1 JC16 are specifically involved in its interaction with tetherin	PubMed
	nef	Tetherin upregulation in HIV-1-infected macrophages is HIV-1 Nef dependent, not a direct consequence of type I interferon induction	PubMed
	nef	HIV-1 replication in immature dendritic cells upregulates tetherin independently of Vpu, but in a Nef-dependent manner	PubMed
Pr55(Gag)	gag	HIV-1 Vpu disrupts the co-localization between HIV-1 Gag and tetherin in a Trp-76-dependent manner in HeLa P4-R5 cells	PubMed
	gag	In cells expressing either wild-type or vpu(-) virus, BST-2 and HIV-1 Gag co-localize both along the plasma membrane and in endosomes	PubMed
	gag	BST-2 delays processing of cellular membrane-associated Gag proteins and adversely affects formation of the core structure in HIV-1 particles	PubMed
	gag	The interaction between HIV-1 Gag and TSG101 enhances tetherin recruitment in HeLa cells. Both TSG101 and ALIX binding sites within the p6 domain of Gag enhance tetherin recruitment to Gag assembly sites in T cells	PubMed
	gag	Tetherin potently inhibits release of Fyn(10)fullMA-Gag, which contains the first 10 amino acids of Fyn kinase at the N terminus of Gag, under cholesterol-depleting conditions in HeLa and HT-1080 cells	PubMed
	gag	Tetherin co-localizes with HIV-1 Gag in CD81- and CD63-enriched intracellular virus-containing compartments in macrophages, and that a separate population of tetherin is located in the TGN	PubMed
	gag	Tetherin accumulates with Gag at the contact zone between infected and target cells, but does not prevent the formation of virological synapses	PubMed
	gag	Cell-free virus particles produced from BST-2 and HIV-1(Vpu-) cotransfected 293T cells have a significant accumulation of the pr55Gag precursor and the p40Gag intermediate products, leading to diminish the infectivity of HIV-1 particles	PubMed
Tat	tat	HIV-1 and the viral protein Tat modulate the expression of bone marrow stromal cell antigen 2 (BST2) in immature dendritic cells and monocyte-derived macrophages	PubMed
Vpr	vpr	HIV-1 Vpr downregulates BST2 expression in human glial cells	PubMed
Vpu	vpu	HIV-1 Vpu (membrane proximal basic residues required) increases the levels of a 23-kDa form of unglycosylated tetherin (transmembrane domain required) in the presence of overexpressed SGTA whereby the C-terminus of SGTA is required for this to occur	PubMed
	vpu	HIV-1 (NL4-3) Vpu downregulates BST2 (CD317/Tetherin); downregulation is dependent on the presence of serines at positions 52 and 56 in Vpu	PubMed
	vpu	HIV-1 subtypes A, B, C, D, and G Vpus inhibit tetherin and allow for HIV-1 release	PubMed
	vpu	HIV-1 Vpu antagonizes the effects of BCA2 on HIV-1 particle production in ""tetherin-positive"" cells	PubMed
	vpu	The betaTrCP binding motif DSGxxS of Vpu is required for optimal downregulation of BST-2 and enhancement of virion-release. Vpu serine (S52/S56) mutants are severely impaired for their ability to counteract tetherin antiviral activity	PubMed
	vpu	HIV-1 Vpus from transmission/founder virus clones downregulates BST2 (Tetherin) but do not efficiently downregulate CD4	PubMed
	vpu	HIV-1 Vpu downregulates cell (CEMT4, Primary CD4+ T cells) surface expression of BST2 (tetherin)	PubMed
	vpu	Vpu counteracts BST2 (tetherin) antiviral activity in HIV-1 transduced cells (293T vs 293T stably expressing BST2(tetherin))	PubMed
	vpu	Vpu from most transmission/founder HIV-1 downregulates BST2 and significantly correlates with level of virus release but did not efficiently downregulate CD4	PubMed
	vpu	Vpu-mediated suppresion of IFN-1 production requires engagement and activation of the LILRA4 (ILT7) plasmacytoid dendritic cell receptor by BST2	PubMed
	vpu	Vpu relocalizes/redistributes BST2 outside assembly sites in primary CD4+ T cells and in SupT1 cells expressing the short BST2 isoform	PubMed
	vpu	Vpu-mediated modulation of IFN-1 production by plasmacytoid dendritic cells requires the presence of BST2 on infected donor cells	PubMed
	vpu	HIV-1 Vpu antagonizes BST2 restiction of HIV-1 replication as demonstrated via mathematical modeling	PubMed
	vpu	HIV-1 (NL4-3) Vpu downregulates BST2 via a cullin-RING E3 ubiquitin ligase complex-independent mechanism	PubMed
	vpu	HIV-1 Vpu downregulates BST-2. The transmembrane/ion channel domain and conserved serines in the cytoplasmic domain of Vpu are required for the Vpu-mediated downregulation of BST-2	PubMed
	vpu	HIV-1 Vpu counteracts the tetherin-induced retention of HIV-1(delVpu) virion particles. Vpu colocalizes with tetherin in co-expression cells	PubMed
	vpu	HIV-1 Vpu disrupts the co-localization between HIV-1 Gag and tetherin in a Trp-76-dependent manner in HeLa P4-R5 cells	PubMed
	vpu	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	PubMed
	vpu	HIV-1 Vpu mutations (A19E, E29K, II43,46SL, R49G/T, SN53,55RH, S53N, E58K) derived from HIV-1 infected patients have defects for both CD4 and tetherin downregulation	PubMed
	vpu	HIV-1 Vpu stabilizes human tetherin in African green monkey kidney COS cells and still counteracts the ability of tetherin to suppress virus release	PubMed
	vpu	Expression of HIV-1 Vpu induces co-localization of tetherin with early endosome protein EEA-1 or late endosome protein LAMP-1	PubMed
	vpu	The ability of HIV-1 Vpu to antagonize tetherin is important for the antibody opsonization of HIV-infected cells, which in turn increases FCGRIII (CD16) signaling	PubMed
	vpu	RNAi-knockdown of tetherin, but not CD4 or NTB-A, increases the resistance of HIV-infected cells to antibody-dependent cell-mediated cytotoxicity (ADCC), suggesting Vpu protects infected cells from ADCC as a function of its ability to counteract tetherin	PubMed
	vpu	N-terminally deleted BST-2 inhibits HIV-1 Vpu-defective and wild-type HIV-1 particle release, and the BST-2 mutant impairs its activity to activate NF-kappaB activation	PubMed
	vpu	The 59EXXXLV64 motif in HIV-1 Vpu is required for Vpu-mediated tetherin downregulation. Vpu E/L/V mutant fails to downregulate tetherin but still interact with beta-TrCP2 and HRS (ESCRT-0)	PubMed
	vpu	Vpu requires a functional polyubiquitin/proteasome system for efficient tetherin degradation. K48R ubiquitin mutant partially blocks Vpu-mediated tetherin downregulation	PubMed
	vpu	HIV-1 Vpu proteins from nonpandemic HIV-1 O and P strains are poor mediators of human tetherin downregulation. Vpus from nonpandemic HIV-1 N strains are as good tetherin antagonists as those from pandemic HIV-1 M strains	PubMed
	vpu	HIV-1 Vpu transmembrane mutants A14N and A18N do not support virus release in the presence of CD317, suggesting that Ala residues at position 14 and 18 are required to antagonize CD317	PubMed
	vpu	Vpu interferes with tetherin trafficking to the cell-surface and causes a relocalization of the cellular tetherin with a TGN marker TGN46 in the TGN, suggesting Vpu-mediated antagonism of tetherin involves binding and sequestration of tetherin in the TGN	PubMed
	vpu	The plasma membrane clathrin adaptor protein complex AP-2 (mu2) is required for optimal downregulation of cell surface BST-2 by Vpu	PubMed
	vpu	All three major structural domains (amino-terminal cytoplasmic tail, transmembrane domain, and extracellular coiled-coil domain) of BST-2 are involved in Vpu-mediated antagonism of tetherin	PubMed
	vpu	The residues including 22 to 24 and 34 to 42 of tetherin play a crucial role in the Vpu interaction. I34, L37, and L41 of tetherin are involved in the determination of Vpu susceptibility	PubMed
	vpu	HIV-1 group N Vpu from Togo downregulates both tetherin isoforms. HIV-2 Env, SIVmac Nef, and KSHV K5 target tetherin isoforms with equal efficiency	PubMed
	vpu	Biotinylation technique in living cells demonstrates that HIV-1 Vpu-induced ER-to-cytosol retro-translocation of tetherin is first exposed to the cytosol as a dimeric oxidized complex and then becomes deglycosylated and reduces to monomers	PubMed
	vpu	Individual Vpu proteins isolated from chronically or acutely infected patients differ substantially in their CD4 and tetherin downregulation function at the cell surface	PubMed
	vpu	BiFC assay demonstrates that the cytoplasmic domain (CD) of HIV-1 Vpu physically interacts with both human and rhesus tetherins. The (G/D)DIWK motif in the CD of rhesus tetherin is responsible for the interaction and the functional antagonism by Vpu	PubMed
	vpu	HIV-1 Vpu-mediated BST-2 downregulation is critical for HIV-1 replication and propagation in vivo in a beta-TrCP dependent manner, especially at early times post-infection	PubMed
	vpu	The peptide BST2-TM-P1 competes with BST-2 binding to HIV-1 Vpu, resulting in restoration of the BST-2 level at HeLa-Vpu cell surface	PubMed
	vpu	Rhesus BST2 inhibits the release of HIV-1 from cells and is resistant to HIV-1 Vpu. Transfer of residues 30-45 of human BST2 into rhesus BST2 is sufficient to confer sensitivity to Vpu	PubMed
	vpu	HIV-1 Vpu interacts with CD317 via its transmembrane region (amino acids 4-27) in living cells	PubMed
	vpu	Alternative translation initiation produces two isoforms of tetherin, l-isoform and s-isoform, which restrict HIV-1 (Vpu-) particle release, but only l-isoform is sentitive to counteraction by Vpu	PubMed
	vpu	Human-monkey tetherin chimeras reveal that the transmembrane domains (amino acids I33V, I36L, P40L, and T45I) of tetherin are determinants of sensitivity/resistance to Vpu	PubMed
	vpu	The cytoplasmic tail of HIV-1 Vpu, specifically within the cytoplasmic tail hinge region (amino acids 47-60), are required for downregulation of both human tetherin and gibbon ape leukemia virus envelope (GaLV Env)	PubMed
	vpu	Chimeras between the TMD of HIV-1 M Vpu and the cytoplasmic domains of SIVcpzPtt, SIVcpzPts, and SIVgor Vpu proteins are capable of counteracting human tetherin to enhance virion release	PubMed
	vpu	The C-terminal alpha-helix (H2) of HIV-1 Vpu cytoplasmic tail domain (CTD) is sufficient to remove tetherin from sites of viral assembly and is necessary for full tetherin antagonist activity	PubMed
	vpu	The residues Q2, P3, I4, A7, V20, V21, V25, I26, and I27 of the TM domain in HIV-1 Vpu form crosslinks with the residues LLL22-4, G27, I28, L29, P40, L41, I43, F44, T45, and I46 of the TM domain in tetherin	PubMed
	vpu	Tetherin is in lipid rafts at the cell surface. Expression of HIV-1 Vpu relocalizes tetherin from the lipid rafts to intracellular endosome and lysosome compartments	PubMed
	vpu	Amino acid substitution variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations maintain its ability to restrict virion release but do not confer resistance to HIV-1 Vpu or SIVtan Env	PubMed
	vpu	HIV-1 Vpu proteins from Cameroonian group N viruses are largely unable to downregulate tetherin. Four amino acid substitutions (E15A, V19A and IV25/26LL) in the transmembrane domain of N-Vpu allow efficient interaction with human tetherin	PubMed
	vpu	HIV-1 Vpu inhibits endogenous expression BST2-induced NF-kappaB activity in cells, and the inhibition requires the beta-TrCP binding motif (residues 51-56; DSGxxS) in Vpu	PubMed
	vpu	HIV-1 Vpu variants from the group C show moderate virus release activity in comparison to group B Vpu variants. The TM domain from the inactive Vpu C is responsible for a significant decrease in egress activity and BST-2 downregulation	PubMed
	vpu	A combination of molecular dynamics simulations and docking approaches shows the lowest energy structure of Vpu-BST2, indicating that Leu-11/14/19/23 and Ile-10/15/18 in BST2 interact with the alanine rim (Ala-8/11/15/19) of Vpu	PubMed
	vpu	Analysis of the chimera HIV-1 Vpu proteins from group M and O shows that alanine-18 is important for group M Vpu localization and tetherin-Vpu interaction	PubMed
	vpu	Overexpression of BST2 and downregulation of HIV-1 Vpu in HIV-1 infected TZM-bl cells inhibit HIV-1 replication	PubMed
	vpu	The retention of HIV-1 Vpu from group O in ER-associated compartments confers a defect to antagonism even when interaction with tetherin is mediated through a chimeric TM domain	PubMed
	vpu	Tetherin delGPI mutant directly interacts with HIV-1 Vpu and inhibits Vpu-induced degradation of tetherin and CD4. Transient expression of tetherin delGPI mutant also inhibits infectious HIV-1 release in tetherin-positive cells	PubMed
	vpu	HIV-1 Vpu downregulates cell-surface BST-2 levels without qualitatively affecting the distribution of the restriction factor at the plasma membrane in HIV-1-infected Jurkat cells	PubMed
	vpu	SCYL2 inhibits Vpu-induced BST2 and CD4 reduction at the cell surface by suppressing the phosphorylation of Vpu at positions Ser-52 and Ser-56	PubMed
	vpu	HIV-1 Vpu from chimpanzee-adapted HIV-1 JC16 downregulates both human and chimpanzee tetherin proteins as efficiently as that of HIV-1 NL4-3 Vpu	PubMed
	vpu	Alanine-scanning mutagenesis and Ala-to-Leu replacement through the HIV-1 Vpu transmembrane domain (residues 5-28) reveals A14 and W22 are required for tetherin antagonism	PubMed
	vpu	HIV-1 BF recombinant Vpu is associated with increased viral particle production when compared to WT B variant virus in tetherin-expressing cell lines	PubMed
	vpu	HIV-1 Vpu rescues the decreased production of infectious HIV-1 virions and restores the diminished reverse transcriptase activities of the culture supernatants as a result of BST-2 inhibition	PubMed
	vpu	Lysine residues (K18/K21) in tetherin are determinants for Vpu-mediated depletion of tetherin. This depletion, however, is dispenable for potent antagonism of the tetherin-mediated restriction of HIV-1 particle release	PubMed
	vpu	A functional ER-associated degradation pathway is required for Vpu-induced tetherin degradation. P97 ATPase (VCP) knockdown partially impairs Vpu-mediated tetherin degradation	PubMed
	vpu	Tetherin cytoplasmic tail lysine residues (K18 and K21) are ubiquitinated in the presence of HIV-1 Vpu and KSHV K5	PubMed
	vpu	HIV-1 Vpu transmembrane domain mutants V9D and I19D fail to promote HIV-1 virion release and to downregulate cell surface tetherin	PubMed
	vpu	Mutation of a single amino acid (T45I) in the transmembrane region of BST-2 results in insensitivity to HIV-1 Vpu while maintaining antiviral activity	PubMed
	vpu	HIV-1 Vpu co-immunoprecipitates with BST-2 in HEK293T cells and in HeLa Tet-Off cells. Deletion of two leucine residues at positions 22 and 23 in tetherin diminishes its association with Vpu	PubMed
	vpu	HIV-1 Vpu reduces steady-state expression of BST-2 in transfected HeLa cells and in HIV-infected macrophages, but not in HIV-infected CEMx174 and H9 cells	PubMed
	vpu	HIV-1 Vpu-A18H downregulates the expression of BST-2 at the cell surface and enhances virion release inefficiently through a reduced interaction with BST-2	PubMed
	vpu	Tetherin inhibits influenza virus neuraminidase (NA) virus-like particle (VLP) release, which is antagonized by HIV-1 Vpu	PubMed
	vpu	In HIV-1-producing cells, CD317 relocalizes predominantly to TfR-positive recycling endosomes, to EEA1-postive early endosomes, and to gin97-positive trans-Golgi network compartments, with some present on late endocytic structures	PubMed
	vpu	All potential acceptor sites (Ser3, Thr4, Ser5, Cys9, Lys18, Cys20, and Lys21) in the cytoplasmic domain of BST2 contribute to Vpu-induced ubiquitination	PubMed
	vpu	BIT225, HIV-1 Vpu viroporin inhibitor, does not affect Vpu-tetherin interactions	PubMed
	vpu	Reduced HIV-1 release in Rab7A-depleted cells is related to expression of the restriction factor tetherin, suggesting that Rab7A contributes to the mechanism by which Vpu counteracts tetherin and rescues HIV-1 release	PubMed
	vpu	SHIV Vpu proteins can counteract human and rhesus BST-2	PubMed
	vpu	A computer modeling method predicts that the interface is composed of Vpu residues I6, A10, A14, A18, V25 and W22, and BST-2 residues L23, I26, V30, I34, V35, L41, I42, and T45	PubMed
	vpu	Endogenous tetherin cell surface expression in T-cell lines H9, CEM-CCRF and CEM-SS are different and that affects HIV-1 Vpu-mediated tetherin modulation on virus release	PubMed
	vpu	An N-terminal deletion and T45I substitution in the TMD of human tetherin render the protein unresponsive to antagonism by HIV-1 Vpu	PubMed
	vpu	NMR studies reveal that the 10AXXXAXXXAXXXW22 face of the Vpu transmembrane domain (TMD) directly binds to the large hydrophobic residues (aa 22-47) of the tetherin TMD in an anti-parallel manner	PubMed
	vpu	The C-terminal fragment of the clathrin assembly protein AP180 inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env	PubMed
	vpu	Dominant negative dynamin 2 (K44A) acts as an inhibitor of clathrin-mediated endocytosis and that it inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env	PubMed
	vpu	The putative cholesterol recognition amino acid consensus (CRAC) motif (residues 25-31) of HIV-1 Vpu mediates lipid raft association of Vpu, but is dispensable for the downregulation of cell surface BST-2	PubMed
	vpu	Tetherin expression is upregulated following HIV-1 infection of monocytes-derived macrophages and is not fully downregulated by HIV-1 Vpu	PubMed
	vpu	HIV-1 Vpu partially antagonizes the restriction of BST2 on HCV production and release from BST2 expressing Huh7.5 cells	PubMed
	vpu	Downregulation of CD4 and BST2 by HIV-1 Vpu is observed in HIV-1 infected humanized mice	PubMed
	vpu	P40L/T45I mutations in human tetherin leads to drastically decreased susceptibility of the mutant to HIV-1 Vpu, while susceptibility to SIVden Vpu increases to 50%, suggesting that these two residues participate in the species-specific activity of Vpu	PubMed
	vpu	Overexpression of clathrin coat-associated protein AP180 inhibits Vpu-mediated tetherin antagonism but adaptor protein-1, adaptor protein-2, and adaptor protein-3 are dispensable	PubMed
	vpu	HIV-1 Vpu E/L/V mutants interact with tetherin in infected cells and are incorporated into nascent virions in a tetherin-dependent manner	PubMed
	vpu	Mutation of the 59EXXXLV64 motif in HIV-1 Vpu leads to endosomal and surface localization of Vpu and modulates the trafficking of tetherin	PubMed
	vpu	The ubiquitin associated protein 1 (UBAP1)-containing ESCRT-I is essential for degradation of antiviral cell-surface protein such as tetherin (BST-2/CD317) by HIV-1 Vpu	PubMed
	vpu	IFNalpha/ribavirin treatment in vivo induces APOBEC3G, APOBEC3F, and BST-2 expression and results in hyper-mutations in viral genome and A11G/S61A mutations in HIV-1 Vpu. These two mutations in Vpu enhances the interaction between BST-2 and Vpu	PubMed
	vpu	Cholesterol-binding compound amphotericin B methyl ester (AME) inhibits the ability of HIV-1 Vpu to counteract the activity of CD317/BST-2/tetherin	PubMed
	vpu	Deletion of amino acids leucine's 22/23 in BST-2 significantly diminishes its association with Vpu, leading to its resistance to antagonism by Vpu	PubMed
	vpu	Monomeric tetherin and non-glycosylated tetherin are expressed at the cell surface and are sensitive to Vpu-induced downregulation	PubMed
	vpu	HIV-1 Vpu and beta-TrCP co-immunoprecipitate with tetherin	PubMed
	vpu	The v-ATPase VPS4 is required for Vpu-induced cell surface downregulation of BST-2	PubMed
	vpu	HRS interacts with both HIV-1 Vpu and tetherin by co-precipitation analysis	PubMed
	vpu	HRS, an ESCRT-0 complex component, is required for the Vpu-induced downregulation of BST-2, indicating that Vpu-induced BST-2 degradation involves the ESCRT/MVB pathway	PubMed
	vpu	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	PubMed
	vpu	The STS sequence in the cytoplasmic domain of BST2 is required for optimal Vpu-mediated downregulation of BST2 from the cell surface and the counteraction of virion release by Vpu	PubMed
	vpu	HIV-1 Vpu accelerates the turnover of mature endogenous BST-2 in both HeLa and CEMx174 cells. The interference of Vpu with the newly synthesized BST-2 results in the gradual depletion of cell surface BST-2	PubMed
	vpu	CD317 exhibits a fast recycling kinetic that is sensitive to treatment with primaquine, a strong recycling inhibitor. HIV-1 Vpu interferes with the recycling of CD317	PubMed
	vpu	HIV-1 Vpu ion channel mutant S23A binds and antagonizes CD317, indicating that its ion channel function is not correlated with its ability to downregulate cell surface CD317	PubMed
	vpu	HIV-1 Vpu cytoplasmic domain mutants S56G and E59K fail to enhance HIV-1 virion release but can reduce cell surface tetherin, suggesting that downregulation of cell surface tetherin and enhancement of virion release by Vpu are not always correlated	PubMed
capsid	gag	HIV-1 CA mutations, P99A and EE75,76AA, pair in tetherin recruitment to HIV-1 assembly sites	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

STS-T47132 (e-PCR)
- UniSTS:55567

RH78341 (e-PCR)
- UniSTS:19307

STS-R65788 (e-PCR)
- UniSTS:58734

RH80754 (e-PCR)
- UniSTS:89469

SHGC-35522 (e-PCR)
- UniSTS:34738

RH102614 (e-PCR)
- UniSTS:96948

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables metalloendopeptidase inhibitor activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in B cell activation	IEA Inferred from Electronic Annotation more info
involved_in defense response to virus	IBA Inferred from Biological aspect of Ancestor more info
involved_in defense response to virus	IDA Inferred from Direct Assay more info	PubMed
involved_in innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of cell growth	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of cell migration	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of intracellular transport of viral material	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of plasmacytoid dendritic cell cytokine production	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of viral genome replication	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of canonical NF-kappaB signal transduction	HMP more info	PubMed
acts_upstream_of_or_within positive regulation of leukocyte proliferation	TAS Traceable Author Statement more info	PubMed
involved_in regulation of actin cytoskeleton organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to interferon-alpha	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to interferon-beta	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to type II interferon	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to virus	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	IBA Inferred from Biological aspect of Ancestor more info
located_in Golgi apparatus	IDA Inferred from Direct Assay more info
located_in apical plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in azurophil granule membrane	TAS Traceable Author Statement more info
is_active_in cell surface	IBA Inferred from Biological aspect of Ancestor more info
located_in cell surface	IMP Inferred from Mutant Phenotype more info	PubMed
located_in cell surface	ISS Inferred from Sequence or Structural Similarity more info
colocalizes_with cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular exosome	HDA more info	PubMed
located_in intracellular membrane-bounded organelle	IDA Inferred from Direct Assay more info
located_in membrane	HDA more info	PubMed
located_in membrane raft	IEA Inferred from Electronic Annotation more info
located_in multivesicular body	IMP Inferred from Mutant Phenotype more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	TAS Traceable Author Statement more info
located_in side of membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: bone marrow stromal antigen 2

Names: BST-2; HM1.24 antigen; NPC-A-7; antiviral factor tetherin

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.