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Q10589 (BST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone marrow stromal antigen 2

Short name=BST-2
Alternative name(s):
HM1.24 antigen
Tetherin
CD_antigen=CD317
Gene names
Name:BST2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, and paramyxoviridae: nipah virus. Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities. Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu. Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2. Ref.10 Ref.11 Ref.12 Ref.15 Ref.17 Ref.20 Ref.22 Ref.23 Ref.24 Ref.30 Ref.31 Ref.34 Ref.36 Ref.38 Ref.39 Ref.41

Subunit structure

Parallel homodimer; disulfide-linked. May form homotetramers under reducing conditions. Isoform 1 and isoform 2 form homodimers and also heterodimers with each other. Dimerization is essential for its antiviral activity. Interacts (via cytoplasmic domain) with ARHGAP44 By similarity. Interacts with MMP14 (via C-terminal cytoplasmic tail). Interacts with LILRA4/ILT7. Interacts (via transmembrane domain) with HIV-1 VPU (via transmembrane domain). Interacts with HIV-2 ENV and ebola GP protein. Ref.2 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.34 Ref.36 Ref.39 Ref.40 Ref.41

Subcellular location

Golgi apparatustrans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchorGPI-anchor. Late endosome. Membrane raft. Cytoplasm. Apical cell membrane By similarity. Note: Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. HIV-1 VPU and HIV-2 ENV can target it to the trans-Golgi network thus sequestering it away from virus assembly sites on the cell membrane. Targeted to late endosomes upon KSHV infection and subsequent ubiquitination. Forms a complex with MMP14 and localizes to the cytoplasm. Ref.12 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 Ref.34 Ref.39

Tissue specificity

Predominantly expressed in liver, lung, heart and placenta. Lower levels in pancreas, kidney, skeletal muscle and brain. Overexpressed in multiple myeloma cells. Highly expressed during B-cell development, from pro-B precursors to plasma cells. Highly expressed on T-cells, monocytes, NK cells and dendritic cells (at protein level). Ref.2 Ref.8

Induction

By type I interferons. Down-regulated by viral antagonistic factors which include: HIV-1 VPU protein, HIV-2 ENV protein, KSHV K5 protein and ebola virus GP protein. VPU and ENV antagonize its function by targeting it to the trans-Golgi network, sequestering it away from virus assembly sites on the cell membrane. VPU also acts as an adapter molecule linking it to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, inducing its ubiquitination and subsequent proteasomal degradation. K5 ubiquitinates it leading to its targeting to late endosomes and degradation. Ref.8 Ref.14 Ref.18 Ref.20 Ref.36

Domain

The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading. Ref.39

Post-translational modification

Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5, leading to its targeting to late endosomes and degradation.

The GPI anchor is essential for its antiviral activity.

Miscellaneous

Tetherin shows evidence of positive (adaptive) selection, presumably as a result of evolutionary pressure applied by antagonistic viral proteins that counteract its inhibitiory activity and this has led to the species-specific tetherin sensitivity to viral countermeasures. For example, Tantalus monkey tetherin cannot be abrogated by HIV-1 VPU due to variation in the tetherin transmembrane region. Similarly, SIV Nefs are able to overcome simian tetherins, but not human tetherin, due to a unique 5-amino-acid deletion in the cytoplasmic tail domain of human tetherin (Ref.13).

Sequence similarities

Belongs to the tetherin family.

Ontologies

Keywords
   Biological processAntiviral defense
B-cell activation
Immunity
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityAlternative initiation
Polymorphism
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Isopeptide bond
Lipoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

defense response to virus

Inferred from direct assay Ref.39. Source: UniProtKB

humoral immune response

Traceable author statement Ref.1. Source: ProtInc

innate immune response

Inferred from direct assay Ref.17. Source: UniProtKB

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

negative regulation of cell growth

Inferred from direct assay Ref.34. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay Ref.34. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from direct assay Ref.34. Source: GOC

negative regulation of intracellular transport of viral material

Inferred from direct assay Ref.17Ref.22Ref.23. Source: UniProtKB

negative regulation of plasmacytoid dendritic cell cytokine production

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-alpha

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-beta

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-gamma

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from direct assay Ref.17Ref.22Ref.23. Source: UniProtKB

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

late endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.17Ref.39Ref.22Ref.23. Source: UniProtKB

   Molecular_functionmetalloendopeptidase inhibitor activity

Inferred from direct assay Ref.34. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15Ref.34. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.39. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q10589-1)

Also known as: l-Tetherin;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q10589-2)

Also known as: s-Tetherin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
Note: Produced by alternative initiation at Met-13 of isoform 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Bone marrow stromal antigen 2
PRO_0000065005
Propeptide162 – 18019Removed in mature form Potential
PRO_0000253552

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4828Helical; Signal-anchor for type II membrane protein; Potential
Topological domain49 – 161113Extracellular Potential
Coiled coil68 – 15285

Amino acid modifications

Lipidation1611GPI-anchor amidated serine Potential
Glycosylation651N-linked (GlcNAc...) Ref.12 Ref.16 Ref.19 Ref.21
Glycosylation921N-linked (GlcNAc...) Ref.12 Ref.21
Disulfide bond53Interchain Ref.12 Ref.21 Ref.39 Ref.40 Ref.41
Disulfide bond63Interchain Ref.12 Ref.21 Ref.39 Ref.40 Ref.41
Disulfide bond91Interchain Ref.12 Ref.21 Ref.39 Ref.40 Ref.41
Cross-link18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24

Natural variations

Alternative sequence1 – 1212Missing in isoform 2.
VSP_053250
Natural variant1431V → F.
Corresponds to variant rs1804402 [ dbSNP | Ensembl ].
VAR_012067

Experimental info

Mutagenesis3 – 53STS → AAA: Partial resistance to Vpu. Ref.36
Mutagenesis61Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-8. Ref.36
Mutagenesis81Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-6. Ref.36
Mutagenesis181K → R: Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. Ref.24
Mutagenesis211K → R: No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. Ref.24
Mutagenesis651N → A: Loss of glycosylation site. Ref.12
Mutagenesis921N → A: Loss of glycosylation site. Impairs anti-viral activity. Ref.12
Sequence conflict1411N → D in BAD96844. Ref.4

Secondary structure

....... 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (l-Tetherin) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CAF52340D69061EE

FASTA18019,769
        10         20         30         40         50         60 
MASTSYDYCR VPMEDGDKRC KLLLGIGILV LLIIVILGVP LIIFTIKANS EACRDGLRAV 

        70         80         90        100        110        120 
MECRNVTHLL QQELTEAQKG FQDVEAQAAT CNHTVMALMA SLDAEKAQGQ KKVEELEGEI 

       130        140        150        160        170        180 
TTLNHKLQDA SAEVERLRRE NQVLSVRIAD KKYYPSSQDS SSAAAPQLLI VLLGLSALLQ 

« Hide

Isoform 2 (s-Tetherin) [UniParc].

Checksum: 965DC8B8EC416C94
Show »

FASTA16818,394

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth."
Ishikawa J., Kaisho T., Tomizawa H., Lee B.O., Kobune Y., Inazawa J., Oritani K., Itoh M., Ochi T., Ishihara K., Hirano T.
Genomics 26:527-534(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells."
Ohtomo T., Sugamata Y., Ozaki Y., Ono K., Yoshimura Y., Kawai S., Koishihara Y., Ozaki S., Kosaka M., Hirano T., Tsuchiya M.
Biochem. Biophys. Res. Commun. 258:583-591(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBUNIT.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Blood.
[8]"Characterization of antibodies submitted to the B cell section of the 8th Human Leukocyte Differentiation Antigens Workshop by flow cytometry and immunohistochemistry."
Vidal-Laliena M., Romero X., March S., Requena V., Petriz J., Engel P.
Cell. Immunol. 236:6-16(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY B-CELL ACTIVATION, NOMENCLATURE.
[9]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein."
Van Damme N., Goff D., Katsura C., Jorgenson R.L., Mitchell R., Johnson M.C., Stephens E.B., Guatelli J.
Cell Host Microbe 3:245-252(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 INFECTION.
[11]"Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu."
Neil S.J., Zang T., Bieniasz P.D.
Nature 451:425-430(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 INFECTION.
[12]"Tetherin inhibits HIV-1 release by directly tethering virions to cells."
Perez-Caballero D., Zang T., Ebrahimi A., McNatt M.W., Gregory D.A., Johnson M.C., Bieniasz P.D.
Cell 139:499-511(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 INFECTION, GLYCOSYLATION AT ASN-65 AND ASN-92, SUBCELLULAR LOCATION, DISULFIDE BONDS, SUBUNIT, TOPOLOGY, GPI-ANCHOR, MUTAGENESIS OF ASN-65 AND ASN-92.
[13]"A tail of Tetherin: how pandemic HIV-1 conquered the world."
Gupta R.K., Towers G.J.
Cell Host Microbe 6:393-395(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes."
Iwabu Y., Fujita H., Kinomoto M., Kaneko K., Ishizaka Y., Tanaka Y., Sata T., Tokunaga K.
J. Biol. Chem. 284:35060-35072(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPU, INDUCTION BY HIV-1 VPU.
[15]"Regulation of TLR7/9 responses in plasmacytoid dendritic cells by BST2 and ILT7 receptor interaction."
Cao W., Bover L., Cho M., Wen X., Hanabuchi S., Bao M., Rosen D.B., Wang Y.H., Shaw J.L., Du Q., Li C., Arai N., Yao Z., Lanier L.L., Liu Y.J.
J. Exp. Med. 206:1603-1614(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LILRA4/ILT7.
[16]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
Tissue: Liver.
[17]"Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin."
Jouvenet N., Neil S.J., Zhadina M., Zang T., Kratovac Z., Lee Y., McNatt M., Hatziioannou T., Bieniasz P.D.
J. Virol. 83:1837-1844(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein."
Le Tortorec A., Neil S.J.
J. Virol. 83:11966-11978(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-2 ENV, SUBCELLULAR LOCATION, INDUCTION BY HIV-2 ENV.
[19]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
Tissue: Leukemic T-cell.
[20]"Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein."
Kaletsky R.L., Francica J.R., Agrawal-Gamse C., Bates P.
Proc. Natl. Acad. Sci. U.S.A. 106:2886-2891(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EBOLA GP PROTEIN, INDUCTION BY EBOLA GP PROTEIN.
[21]"The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu."
Andrew A.J., Miyagi E., Kao S., Strebel K.
Retrovirology 6:80-80(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-65 AND ASN-92, SUBUNIT, DISULFIDE BONDS.
[22]"Infectious Lassa virus, but not filoviruses, is restricted by BST-2/tetherin."
Radoshitzky S.R., Dong L., Chi X., Clester J.C., Retterer C., Spurgers K., Kuhn J.H., Sandwick S., Ruthel G., Kota K., Boltz D., Warren T., Kranzusch P.J., Whelan S.P., Bavari S.
J. Virol. 84:10569-10580(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[23]"Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms."
Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.
J. Virol. 84:12646-12657(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[24]"The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin."
Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P., Kellam P., Towers G.J., Neil S.J.
PLoS Pathog. 6:E1000843-E1000843(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN KSHV AND HIV-1 INFECTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-18 AND LYS-21, UBIQUITINATION AT LYS-18 BY KSH VIRUS E3 UBIQUITIN-PROTEIN LIGASE K5.
[25]"BST-2/tetherin: a new component of the innate immune response to enveloped viruses."
Evans D.T., Serra-Moreno R., Singh R.K., Guatelli J.C.
Trends Microbiol. 18:388-396(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"structural basis for the antiviral activity of Bst-2/tetherin and its viral antagonism."
Arias J.F., Iwabu Y., Tokunaga K.
Front. Microbiol. 2:250-250(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"The interferon-inducible host factor bone marrow stromal antigen 2/tetherin restricts virion release, but is it actually a viral restriction factor?"
Andrew A., Strebel K.
J. Interferon Cytokine Res. 31:137-144(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[29]"Tetherin and its viral antagonists."
Kuhl B.D., Cheng V., Wainberg M.A., Liang C.
J. Neuroimmun. Pharmacol. 6:188-201(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[30]"Tetherin inhibits prototypic foamy virus release."
Xu F., Tan J., Liu R., Xu D., Li Y., Geng Y., Liang C., Qiao W.
Virol. J. 8:198-198(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin."
Watanabe R., Leser G.P., Lamb R.A.
Virology 417:50-56(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"Antiviral inhibition of enveloped virus release by tetherin/BST-2: action and counteraction."
Le Tortorec A., Willey S., Neil S.J.
Viruses 3:520-540(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[33]"Vpu and BST2: still not there yet?"
Sato K., Gee P., Koyanagi Y.
Front. Microbiol. 3:131-131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[34]"BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity."
Gu G., Zhao D., Yin Z., Liu P.
J. Cell. Biochem. 113:1013-1021(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MMP14.
[35]"Restriction of retroviral replication by tetherin/BST-2."
Hammonds J., Wang J.J., Spearman P.
Mol. Biol. Int. 2012:424768-424768(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[36]"Identification of alternatively translated Tetherin isoforms with differing antiviral and signaling activities."
Cocka L.J., Bates P.
PLoS Pathog. 8:E1002931-E1002931(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, ALTERNATIVE INITIATION (ISOFORMS 1 AND 2), INDUCTION, MUTAGENESIS OF 3-SER--SER-5; TYR-6 AND TYR-8.
[37]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Modulation of hepatitis C virus release by the interferon-induced protein BST-2/tetherin."
Dafa-Berger A., Kuzmina A., Fassler M., Yitzhak-Asraf H., Shemer-Avni Y., Taube R.
Virology 428:98-111(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[39]"Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain."
Hinz A., Miguet N., Natrajan G., Usami Y., Yamanaka H., Renesto P., Hartlieb B., McCarthy A.A., Simorre J.P., Gottlinger H., Weissenhorn W.
Cell Host Microbe 7:314-323(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 87-147, FUNCTION, DOMAIN, DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION, CIRCULAR DICHROISM.
[40]"Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations."
Schubert H.L., Zhai Q., Sandrin V., Eckert D.M., Garcia-Maya M., Saul L., Sundquist W.I., Steiner R.A., Hill C.P.
Proc. Natl. Acad. Sci. U.S.A. 107:17951-17956(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 47-152, SUBUNIT, DISULFIDE BONDS.
[41]"Structural insight into the mechanisms of enveloped virus tethering by tetherin."
Yang H., Wang J., Jia X., McNatt M.W., Zang T., Pan B., Meng W., Wang H.W., Bieniasz P.D., Xiong Y.
Proc. Natl. Acad. Sci. U.S.A. 107:18428-18432(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 47-161, SUBUNIT, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28137 mRNA. Translation: BAA05679.1.
AK223124 mRNA. Translation: BAD96844.1.
AK291099 mRNA. Translation: BAF83788.1.
AC010319 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84602.1.
BC033873 mRNA. Translation: AAH33873.1.
CCDSCCDS12358.1. [Q10589-1]
PIRA56836.
RefSeqNP_004326.1. NM_004335.3. [Q10589-1]
UniGeneHs.118110.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LK9NMR-A18-47[»]
2X7AX-ray2.77A/B/C/D/E/F/G/H/I/J/K87-147[»]
2XG7X-ray3.45A/C51-151[»]
3MQ7X-ray2.28A/B/C/D/E/F/G/H/I/J/K/L47-161[»]
3MQ9X-ray2.80A/B/C/D/E/F/G/H66-139[»]
3MQBX-ray3.20A/B/E/F47-161[»]
3MQCX-ray2.80A/B/C/D47-161[»]
3NWHX-ray2.60A/B/C/D47-152[»]
4P6ZX-ray3.00T1-21[»]
ProteinModelPortalQ10589.
SMRQ10589. Positions 48-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107149. 11 interactions.
DIPDIP-53216N.
IntActQ10589. 4 interactions.
MINTMINT-8402291.
STRING9606.ENSP00000252593.

PTM databases

PhosphoSiteQ10589.

Polymorphism databases

DMDM1705508.

Proteomic databases

MaxQBQ10589.
PaxDbQ10589.
PeptideAtlasQ10589.
PRIDEQ10589.

Protocols and materials databases

DNASU684.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252593; ENSP00000252593; ENSG00000130303. [Q10589-1]
GeneID684.
KEGGhsa:684.
UCSCuc002ngl.3. human. [Q10589-1]

Organism-specific databases

CTD684.
GeneCardsGC19M017513.
HGNCHGNC:1119. BST2.
HPAHPA017060.
MIM600534. gene.
neXtProtNX_Q10589.
PharmGKBPA25436.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41121.
HOGENOMHOG000013084.
HOVERGENHBG004902.
InParanoidQ10589.
KOK06731.
OMALNHKLQD.
OrthoDBEOG7D59R5.
PhylomeDBQ10589.
TreeFamTF338345.

Gene expression databases

BgeeQ10589.
CleanExHS_BST2.
GenevestigatorQ10589.

Family and domain databases

InterProIPR024886. BST2.
[Graphical view]
PANTHERPTHR15190. PTHR15190. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ10589.
GeneWikiTetherin.
GenomeRNAi684.
NextBio2816.
PROQ10589.
SOURCESearch...

Entry information

Entry nameBST2_HUMAN
AccessionPrimary (citable) accession number: Q10589
Secondary accession number(s): A8K4Y4, Q53G07
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries