Q10589 (BST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bone marrow stromal antigen 2
Short name=BST-2

Alternative name(s):
HM1.24 antigen
Tetherin
CD_antigen=CD317

Gene names

Name:

BST2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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.37 Ref.39
Subunit structure	Parallel homodimer; disulfide-linked. May form homotetramers under reducing conditions. 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.37 Ref.38 Ref.39
Subcellular location	Golgi apparatus › trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor › GPI-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.37
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
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.37
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 process	Antiviral defense B-cell activation Immunity Innate immunity
Cellular component	Cell membrane Cytoplasm Endosome Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond GPI-anchor Glycoprotein Isopeptide bond Lipoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B 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.37. Source: UniProtKB humoral immune response Traceable author statement Ref.1. Source: ProtInc 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 egress of virus within host cell 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 cascade 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
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell anchored to 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 integral to 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
Molecular_function	metalloendopeptidase inhibitor activity Inferred from direct assay Ref.34. Source: UniProtKB signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 161

161

Bone marrow stromal antigen 2

PRO_0000065005

Propeptide

162 – 180

19

Removed in mature form Potential

PRO_0000253552

Regions

Topological domain

1 – 20

20

Cytoplasmic Potential

Transmembrane

21 – 48

28

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

49 – 161

113

Extracellular Potential

Coiled coil

68 – 152

85

Amino acid modifications

Lipidation

161

1

GPI-anchor amidated serine Potential

Glycosylation

65

1

N-linked (GlcNAc...) Ref.12 Ref.16 Ref.19 Ref.21

Glycosylation

92

1

N-linked (GlcNAc...) Ref.12 Ref.21

Disulfide bond

53

Interchain Ref.12 Ref.21 Ref.37 Ref.38 Ref.39

Disulfide bond

63

Interchain Ref.12 Ref.21 Ref.37 Ref.38 Ref.39

Disulfide bond

91

Interchain Ref.12 Ref.21 Ref.37 Ref.38 Ref.39

Cross-link

18

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24

Natural variations

Natural variant

143

1

V → F.
Corresponds to variant rs1804402 [ dbSNP | Ensembl ].

VAR_012067

Experimental info

Mutagenesis

18

1

K → R: Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. Ref.24

Mutagenesis

21

1

K → R: No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. Ref.24

Mutagenesis

65

1

N → A: Loss of glycosylation site. Ref.12

Mutagenesis

92

1

N → A: Loss of glycosylation site. Impairs anti-viral activity. Ref.12

Sequence conflict

141

1

N → D in BAD96844. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

180

Helix Strand Turn

Details...

Helix

23 – 44

22

Helix

52 – 148

97

Beta strand

152 – 154

3

Sequences

	Sequence		Length	Mass (Da)
	Q10589 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CAF52340D69061EE	FASTA	180	19,769
	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

References

	« Hide 'large scale' referencesShow '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].
[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], 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. , 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].
[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].
[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. , 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. , 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]. 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
[37]	"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.
[38]	"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.
[39]	"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.

IPI

IPI00026241.

PIR

A56836.

RefSeq

NP_004326.1. NM_004335.2.

UniGene

Hs.118110.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LK9	NMR	-	A	18-47	[»]
2X7A	X-ray	2.77	A/B/C/D/E/F/G/H/I/J/K	87-147	[»]
2XG7	X-ray	3.45	A/C	51-151	[»]
3MQ7	X-ray	2.28	A/B/C/D/E/F/G/H/I/J/K/L	47-161	[»]
3MQ9	X-ray	2.80	A/B/C/D/E/F/G/H	66-139	[»]
3MQB	X-ray	3.20	A/B/E/F	47-161	[»]
3MQC	X-ray	2.80	A/B/C/D	47-161	[»]
3NWH	X-ray	2.60	A/B/C/D	47-152	[»]

ProteinModelPortal

Q10589.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-53216N.

IntAct

Q10589. 3 interactions.

MINT

MINT-8402291.

STRING

9606.ENSP00000252593.

PTM databases

PhosphoSite

Q10589.

Polymorphism databases

DMDM

1705508.

Proteomic databases

PaxDb

Q10589.

PeptideAtlas

Q10589.

PRIDE

Q10589.

Protocols and materials databases

DNASU

684.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000252593; ENSP00000252593; ENSG00000130303.

GeneID

684.

KEGG

hsa:684.

UCSC

uc002ngl.3. human.

Organism-specific databases

CTD

684.

GeneCards

GC19M017502.

HGNC

HGNC:1119. BST2.

HPA

HPA017060.

MIM

600534. gene.

neXtProt

NX_Q10589.

PharmGKB

PA25436.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41121.

HOGENOM

HOG000013084.

HOVERGEN

HBG004902.

InParanoid

Q10589.

KO

K06731.

OMA

KDGDKRC.

PhylomeDB

Q10589.

Gene expression databases

Bgee

Q10589.

CleanEx

HS_BST2.

Genevestigator

Q10589.

GermOnline

ENSG00000130303. Homo sapiens.

Family and domain databases

InterPro

IPR024886. BST2.
[Graphical view]

PANTHER

PTHR15190. PTHR15190. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q10589.

GenomeRNAi

684.

NextBio

2816.

SOURCE

Search...

Entry information

Entry name

BST2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.