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Protein

Bone marrow stromal antigen 2

Gene

BST2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:19564354, PubMed:26172439). 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 (PubMed:23028328, PubMed:26172439). Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu (PubMed:23028328, PubMed:26172439). Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2 (PubMed:23028328).17 Publications

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 (PubMed:19917491).1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • identical protein binding Source: IntAct
  • metalloendopeptidase inhibitor activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAntiviral defense, B-cell activation, Immunity, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-6798695 Neutrophil degranulation
R-HSA-909733 Interferon alpha/beta signaling

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bone marrow stromal antigen 2
Short name:
BST-2
Alternative name(s):
HM1.24 antigen
Tetherin
CD_antigen: CD317
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BST2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000130303.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1119 BST2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600534 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q10589

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 20CytoplasmicSequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei21 – 48Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST28
Topological domaini49 – 161ExtracellularSequence analysisAdd BLAST113

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3 – 5STS → AAA: Partial resistance to Vpu. 1 Publication3
Mutagenesisi6Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-8. 1 Publication1
Mutagenesisi8Y → A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-6. 1 Publication1
Mutagenesisi18K → R: Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. 1 Publication1
Mutagenesisi21K → R: No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5. 1 Publication1
Mutagenesisi65N → A: Loss of glycosylation site. 1 Publication1
Mutagenesisi92N → A: Loss of glycosylation site. Impairs anti-viral activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
684

Open Targets

More...
OpenTargetsi
ENSG00000130303

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA25436

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1705508

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000650051 – 161Bone marrow stromal antigen 2Add BLAST161
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000253552162 – 180Removed in mature formSequence analysisAdd BLAST19

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi53Interchain
Disulfide bondi63Interchain
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi65N-linked (GlcNAc...) asparagine4 Publications1
Disulfide bondi91Interchain
Glycosylationi92N-linked (GlcNAc...) asparagine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi161GPI-anchor amidated serineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5, leading to its targeting to late endosomes and degradation.1 Publication
The GPI anchor is essential for its antiviral activity.

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q10589

MaxQB - The MaxQuant DataBase

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MaxQBi
Q10589

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q10589

PeptideAtlas

More...
PeptideAtlasi
Q10589

PRoteomics IDEntifications database

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PRIDEi
Q10589

ProteomicsDB human proteome resource

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ProteomicsDBi
58866

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1044

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q10589

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q10589

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q10589

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000130303 Expressed in 209 organ(s), highest expression level in left ovary

CleanEx database of gene expression profiles

More...
CleanExi
HS_BST2

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q10589 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q10589 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA017060

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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) (PubMed:22065321). Interacts with LILRA4/ILT7 (PubMed:19564354, PubMed:26172439). Interacts (via transmembrane domain) with HIV-1 VPU (via transmembrane domain) (PubMed:19837671). Interacts with HIV-2 ENV and ebola GP protein (PubMed:19740980, PubMed:19179289).By similarity12 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107149, 17 interactors

Database of interacting proteins

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DIPi
DIP-53216N

Protein interaction database and analysis system

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IntActi
Q10589, 18 interactors

Molecular INTeraction database

More...
MINTi
Q10589

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000252593

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q10589

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q10589

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q10589

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili68 – 152Add BLAST85

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the tetherin family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410JE1U Eukaryota
ENOG41115GP LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013782

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000013084

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004902

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q10589

KEGG Orthology (KO)

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KOi
K06731

Identification of Orthologs from Complete Genome Data

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OMAi
LNHKLQD

Database of Orthologous Groups

More...
OrthoDBi
EOG091G1B7U

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q10589

TreeFam database of animal gene trees

More...
TreeFami
TF338345

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024886 BST2

The PANTHER Classification System

More...
PANTHERi
PTHR15190 PTHR15190, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16716 BST2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
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
        10         20         30         40         50
MASTSYDYCR VPMEDGDKRC KLLLGIGILV LLIIVILGVP LIIFTIKANS
60 70 80 90 100
EACRDGLRAV MECRNVTHLL QQELTEAQKG FQDVEAQAAT CNHTVMALMA
110 120 130 140 150
SLDAEKAQGQ KKVEELEGEI TTLNHKLQDA SAEVERLRRE NQVLSVRIAD
160 170 180
KKYYPSSQDS SSAAAPQLLI VLLGLSALLQ
Length:180
Mass (Da):19,769
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti141N → D in BAD96844 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012067143V → F. Corresponds to variant dbSNP:rs1804402Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0532501 – 12Missing in isoform 2. CuratedAdd BLAST12

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS12358.1 [Q10589-1]

Protein sequence database of the Protein Information Resource

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PIRi
A56836

NCBI Reference Sequences

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RefSeqi
NP_004326.1, NM_004335.3 [Q10589-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.118110

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000252593; ENSP00000252593; ENSG00000130303 [Q10589-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
684

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:684

UCSC genome browser

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UCSCi
uc060vid.1 human [Q10589-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
6CM9electron microscopy3.73L/N/T2-21[»]
6CRIelectron microscopy6.80N/T/Y/Z/c/d2-21[»]
6D83electron microscopy4.27L/T2-21[»]
6D84electron microscopy6.72L/O/R/T2-21[»]
6DFFelectron microscopy3.90L/T2-21[»]
ProteinModelPortaliQ10589
SMRiQ10589
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107149, 17 interactors
DIPiDIP-53216N
IntActiQ10589, 18 interactors
MINTiQ10589
STRINGi9606.ENSP00000252593

PTM databases

GlyConnecti1044
iPTMnetiQ10589
PhosphoSitePlusiQ10589
SwissPalmiQ10589

Polymorphism and mutation databases

DMDMi1705508

Proteomic databases

EPDiQ10589
MaxQBiQ10589
PaxDbiQ10589
PeptideAtlasiQ10589
PRIDEiQ10589
ProteomicsDBi58866

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
684
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252593; ENSP00000252593; ENSG00000130303 [Q10589-1]
GeneIDi684
KEGGihsa:684
UCSCiuc060vid.1 human [Q10589-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
684
DisGeNETi684
EuPathDBiHostDB:ENSG00000130303.12

GeneCards: human genes, protein and diseases

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GeneCardsi
BST2
HGNCiHGNC:1119 BST2
HPAiHPA017060
MIMi600534 gene
neXtProtiNX_Q10589
OpenTargetsiENSG00000130303
PharmGKBiPA25436

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiENOG410JE1U Eukaryota
ENOG41115GP LUCA
GeneTreeiENSGT00390000013782
HOGENOMiHOG000013084
HOVERGENiHBG004902
InParanoidiQ10589
KOiK06731
OMAiLNHKLQD
OrthoDBiEOG091G1B7U
PhylomeDBiQ10589
TreeFamiTF338345

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-909733 Interferon alpha/beta signaling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
BST2 human
EvolutionaryTraceiQ10589

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Tetherin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
684

Protein Ontology

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PROi
PR:Q10589

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000130303 Expressed in 209 organ(s), highest expression level in left ovary
CleanExiHS_BST2
ExpressionAtlasiQ10589 baseline and differential
GenevisibleiQ10589 HS

Family and domain databases

InterProiView protein in InterPro
IPR024886 BST2
PANTHERiPTHR15190 PTHR15190, 1 hit
PfamiView protein in Pfam
PF16716 BST2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBST2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q10589
Secondary accession number(s): A8K4Y4, Q53G07
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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