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Q10589

- BST2_HUMAN

UniProt

Q10589 - BST2_HUMAN

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Protein
Bone marrow stromal antigen 2
Gene
BST2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 2.16 Publications

GO - Molecular functioni

  1. metalloendopeptidase inhibitor activity Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB-KW
  2. cell proliferation Source: ProtInc
  3. cell-cell signaling Source: ProtInc
  4. defense response to virus Source: UniProtKB
  5. humoral immune response Source: ProtInc
  6. innate immune response Source: UniProtKB
  7. multicellular organismal development Source: ProtInc
  8. negative regulation of cell growth Source: UniProtKB
  9. negative regulation of cell migration Source: UniProtKB
  10. negative regulation of endopeptidase activity Source: GOC
  11. negative regulation of intracellular transport of viral material Source: UniProtKB
  12. negative regulation of plasmacytoid dendritic cell cytokine production Source: UniProtKB
  13. negative regulation of viral genome replication Source: UniProtKB
  14. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  15. regulation of actin cytoskeleton organization Source: UniProtKB
  16. response to interferon-alpha Source: UniProtKB
  17. response to interferon-beta Source: UniProtKB
  18. response to interferon-gamma Source: UniProtKB
  19. response to virus Source: UniProtKB
  20. signal transduction Source: GOC
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, B-cell activation, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Bone marrow stromal antigen 2
Short name:
BST-2
Alternative name(s):
HM1.24 antigen
Tetherin
CD_antigen: CD317
Gene namesi
Name:BST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1119. BST2.

Subcellular locationi

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.8 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei21 – 4828Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini49 – 161113Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. anchored component of membrane Source: UniProtKB-KW
  3. apical plasma membrane Source: UniProtKB
  4. cell surface Source: UniProtKB
  5. cytoplasm Source: HPA
  6. extracellular vesicular exosome Source: UniProt
  7. integral component of plasma membrane Source: ProtInc
  8. late endosome Source: UniProtKB-SubCell
  9. membrane raft Source: UniProtKB-SubCell
  10. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 53STS → AAA: Partial resistance to Vpu. 1 Publication
Mutagenesisi6 – 61Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-8. 1 Publication
Mutagenesisi8 – 81Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-6. 1 Publication
Mutagenesisi18 – 181K → R: Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. 1 Publication
Mutagenesisi21 – 211K → R: No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. 1 Publication
Mutagenesisi65 – 651N → A: Loss of glycosylation site. 1 Publication
Mutagenesisi92 – 921N → A: Loss of glycosylation site. Impairs anti-viral activity. 1 Publication

Organism-specific databases

PharmGKBiPA25436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Bone marrow stromal antigen 2
PRO_0000065005Add
BLAST
Propeptidei162 – 18019Removed in mature form Reviewed prediction
PRO_0000253552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Disulfide bondi53 – 53Interchain5 Publications
Disulfide bondi63 – 63Interchain5 Publications
Glycosylationi65 – 651N-linked (GlcNAc...)4 Publications
Disulfide bondi91 – 91Interchain5 Publications
Glycosylationi92 – 921N-linked (GlcNAc...)2 Publications
Lipidationi161 – 1611GPI-anchor amidated serine Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Isopeptide bond, Lipoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ10589.
PaxDbiQ10589.
PeptideAtlasiQ10589.
PRIDEiQ10589.

PTM databases

PhosphoSiteiQ10589.

Expressioni

Tissue specificityi

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).2 Publications

Inductioni

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.5 Publications

Gene expression databases

BgeeiQ10589.
CleanExiHS_BST2.
GenevestigatoriQ10589.

Organism-specific databases

HPAiHPA017060.

Interactioni

Subunit structurei

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.12 Publications

Protein-protein interaction databases

BioGridi107149. 11 interactions.
DIPiDIP-53216N.
IntActiQ10589. 4 interactions.
MINTiMINT-8402291.
STRINGi9606.ENSP00000252593.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 4422
Helixi52 – 14897
Beta strandi152 – 1543

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ10589.
SMRiQ10589. Positions 48-152.

Miscellaneous databases

EvolutionaryTraceiQ10589.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili68 – 15285
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the tetherin family.

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41121.
HOGENOMiHOG000013084.
HOVERGENiHBG004902.
InParanoidiQ10589.
KOiK06731.
OMAiLNHKLQD.
OrthoDBiEOG7D59R5.
PhylomeDBiQ10589.
TreeFamiTF338345.

Family and domain databases

InterProiIPR024886. BST2.
[Graphical view]
PANTHERiPTHR15190. PTHR15190. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: Q10589-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MASTSYDYCR VPMEDGDKRC KLLLGIGILV LLIIVILGVP LIIFTIKANS    50
EACRDGLRAV MECRNVTHLL QQELTEAQKG FQDVEAQAAT CNHTVMALMA 100
SLDAEKAQGQ KKVEELEGEI TTLNHKLQDA SAEVERLRRE NQVLSVRIAD 150
KKYYPSSQDS SSAAAPQLLI VLLGLSALLQ 180
Length:180
Mass (Da):19,769
Last modified:October 1, 1996 - v1
Checksum:iCAF52340D69061EE
GO
Isoform 2 (identifier: Q10589-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:168
Mass (Da):18,394
Checksum:i965DC8B8EC416C94
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431V → F.
Corresponds to variant rs1804402 [ dbSNP | Ensembl ].
VAR_012067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212Missing in isoform 2.
VSP_053250Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411N → D in BAD96844. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12358.1. [Q10589-1]
PIRiA56836.
RefSeqiNP_004326.1. NM_004335.3. [Q10589-1]
UniGeneiHs.118110.

Genome annotation databases

EnsembliENST00000252593; ENSP00000252593; ENSG00000130303. [Q10589-1]
GeneIDi684.
KEGGihsa:684.
UCSCiuc002ngl.3. human. [Q10589-1]

Polymorphism databases

DMDMi1705508.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12358.1. [Q10589-1 ]
PIRi A56836.
RefSeqi NP_004326.1. NM_004335.3. [Q10589-1 ]
UniGenei Hs.118110.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4P6Z X-ray 3.00 T 1-21 [» ]
ProteinModelPortali Q10589.
SMRi Q10589. Positions 48-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107149. 11 interactions.
DIPi DIP-53216N.
IntActi Q10589. 4 interactions.
MINTi MINT-8402291.
STRINGi 9606.ENSP00000252593.

PTM databases

PhosphoSitei Q10589.

Polymorphism databases

DMDMi 1705508.

Proteomic databases

MaxQBi Q10589.
PaxDbi Q10589.
PeptideAtlasi Q10589.
PRIDEi Q10589.

Protocols and materials databases

DNASUi 684.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252593 ; ENSP00000252593 ; ENSG00000130303 . [Q10589-1 ]
GeneIDi 684.
KEGGi hsa:684.
UCSCi uc002ngl.3. human. [Q10589-1 ]

Organism-specific databases

CTDi 684.
GeneCardsi GC19M017513.
HGNCi HGNC:1119. BST2.
HPAi HPA017060.
MIMi 600534. gene.
neXtProti NX_Q10589.
PharmGKBi PA25436.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41121.
HOGENOMi HOG000013084.
HOVERGENi HBG004902.
InParanoidi Q10589.
KOi K06731.
OMAi LNHKLQD.
OrthoDBi EOG7D59R5.
PhylomeDBi Q10589.
TreeFami TF338345.

Miscellaneous databases

EvolutionaryTracei Q10589.
GeneWikii Tetherin.
GenomeRNAii 684.
NextBioi 2816.
PROi Q10589.
SOURCEi Search...

Gene expression databases

Bgeei Q10589.
CleanExi HS_BST2.
Genevestigatori Q10589.

Family and domain databases

InterProi IPR024886. BST2.
[Graphical view ]
PANTHERi PTHR15190. PTHR15190. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiBST2_HUMAN
AccessioniPrimary (citable) accession number: Q10589
Secondary accession number(s): A8K4Y4, Q53G07
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

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 (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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