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Q3TBT3

- STING_MOUSE

UniProt

Q3TBT3 - STING_MOUSE

Protein

Stimulator of interferon genes protein

Gene

Tmem173

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei262 – 2621c-di-GMP

    GO - Molecular functioni

    1. cyclic-di-GMP binding Source: UniProtKB
    2. cyclic-GMP-AMP binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein homodimerization activity Source: UniProtKB
    5. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of innate immune response Source: UniProtKB
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to exogenous dsRNA Source: Ensembl
    4. cellular response to interferon-beta Source: MGI
    5. defense response to virus Source: UniProtKB
    6. innate immune response Source: UniProtKB
    7. interferon-beta production Source: UniProtKB
    8. positive regulation of defense response to virus by host Source: Ensembl
    9. positive regulation of protein binding Source: Ensembl
    10. positive regulation of protein import into nucleus, translocation Source: Ensembl
    11. positive regulation of transcription factor import into nucleus Source: Ensembl
    12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    13. positive regulation of type I interferon production Source: InterPro

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
    REACT_196457. STING mediated induction of host immune responses.
    REACT_196519. Regulation of innate immune responses to cytosolic DNA.
    REACT_198980. IRF3 mediated activation of type 1 IFN.
    REACT_227400. STAT6-mediated induction of chemokines.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stimulator of interferon genes protein
    Short name:
    mSTING
    Alternative name(s):
    Endoplasmic reticulum interferon stimulator
    Short name:
    ERIS
    Mediator of IRF3 activation
    Short name:
    MMITA
    Transmembrane protein 173
    Gene namesi
    Name:Tmem173
    Synonyms:Eris Mita, Mpys, Sting
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1919762. Tmem173.

    Subcellular locationi

    Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein. Cytoplasmperinuclear region. Cytoplasm By similarity
    Note: In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. Golgi apparatus Source: MGI
    4. integral component of membrane Source: UniProtKB-KW
    5. mitochondrial outer membrane Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. peroxisome Source: MGI
    8. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Disruption phenotypei

    Defects in innate immunity. Death within 7 days of herpes simplex virus 1 (HSV-1) infection. In addition, mice show a remarkable reduction in cytotoxic T-cell responses after plasmid DNA vaccination. Cells fail to induce type I interferon production in response to dsDNA and infection with herpes simplex virus 1 (HSV-1) and L.monocytogenes that deliver DNA to the host cytosol.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611S → A: Decrease in cGAMP-binding. 1 Publication
    Mutagenesisi239 – 2391Y → S: Strong decrease in cGAMP-binding. 1 Publication
    Mutagenesisi241 – 2411N → A: Strong decrease in cGAMP-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 378378Stimulator of interferon genes proteinPRO_0000271117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki150 – 150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei357 – 3571Phosphoserine; by TBK1By similarity

    Post-translational modificationi

    Phosphorylated on Ser-357 by TBK1, leading to activation and production of IFN-beta By similarity. Phosphorylated on tyrosine residues upon MHC-II aggregation.By similarity1 Publication
    Ubiquitinated. 'Lys-63'-linked ubiquitination mediated by TRIM56 at Lys-150 promotes homodimerization and recruitment of the antiviral kinase TBK1 and subsequent production of IFN-beta. 'Lys-48'-linked polyubiquitination at Lys-150 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ3TBT3.
    PRIDEiQ3TBT3.

    PTM databases

    PhosphoSiteiQ3TBT3.

    Expressioni

    Tissue specificityi

    Present in spleen and thymus tissue. Also present in dendritic cells (at protein level).1 Publication

    Developmental stagei

    Expressed throughout the B-cell lineage prior to the plasma cell stage but occurs at highest levels in mature B-cells. Highly expressed in cells representing mature stages of B-cells but weakly expressed in pre-B cells, immature B-cells, and memory B-cell stages. Not detected in plasma cells.1 Publication

    Gene expression databases

    BgeeiQ3TBT3.
    CleanExiMM_TMEM173.
    GenevestigatoriQ3TBT3.

    Interactioni

    Subunit structurei

    Homodimer; 'Lys-63'-linked ubiquitination at Lys-150 is required for homodimerization. Interacts with TBK1; when homodimer, leading to subsequent production of IFN-beta By similarity. Interacts with DDX58/RIG-I, MAVS and SSR2. Interacts with RNF5. Associates with the MHC-II complex. Interacts with IFIT1 and IFIT2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ddx41Q91VN64EBI-3862093,EBI-2551902
    Tbk1Q9WUN23EBI-3862093,EBI-764193

    Protein-protein interaction databases

    DIPiDIP-59959N.
    IntActiQ3TBT3. 4 interactions.

    Structurei

    Secondary structure

    1
    378
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi156 – 1649
    Helixi167 – 1704
    Turni171 – 1733
    Helixi174 – 18411
    Turni185 – 1895
    Helixi192 – 1943
    Beta strandi195 – 2028
    Helixi211 – 2133
    Beta strandi218 – 2236
    Beta strandi227 – 2315
    Beta strandi234 – 2396
    Beta strandi242 – 2487
    Beta strandi251 – 26010
    Helixi262 – 27211
    Turni274 – 2763
    Helixi280 – 29819
    Helixi304 – 3074
    Beta strandi308 – 3136
    Beta strandi317 – 3193
    Helixi324 – 33310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JC5X-ray2.75A/B149-348[»]
    4KBYX-ray2.36A/B138-344[»]
    4KC0X-ray2.20A/B138-344[»]
    4LOJX-ray1.77A/B154-340[»]
    4LOKX-ray2.07A/B154-340[»]
    4LOLX-ray2.43A/B154-340[»]
    ProteinModelPortaliQ3TBT3.
    SMRiQ3TBT3. Positions 155-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini42 – 465ExtracellularSequence Analysis
    Topological domaini68 – 8619CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini107 – 1148ExtracellularSequence Analysis
    Topological domaini136 – 378243CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei47 – 6721Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei87 – 10620Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei115 – 13521Helical; Name=4Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 339188c-di-GMP-binding domain (CBD)Add
    BLAST
    Regioni161 – 1666c-di-GMP binding
    Regioni237 – 2404c-di-GMP binding
    Regioni339 – 37840C-terminal tail (CTT)By similarityAdd
    BLAST

    Domaini

    The c-di-GMP-binding domain (CBD) forms a homodimer via hydrophobic interactions and binds both the cyclic diguanylate monophosphate (c-di-GMP) and the cyclic GMP-AMP (cGAMP) messengers. In absence of c-di-GMP or cGAMP, the protein is autoinhibited by an intramolecular interaction between the CBD and the C-terminal tail (CTT). Binding of c-di-GMP or cGAMP to the CBD releases the autoinhibition by displacing the CTT, leading to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon. The N-terminal part of the CBD region was initially though to contain a fifth transmembrane region (TM5) but is part of the folded, soluble CBD By similarity.By similarity

    Sequence similaritiesi

    Belongs to the TMEM173 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43926.
    GeneTreeiENSGT00390000008582.
    HOVERGENiHBG094065.
    InParanoidiA7YGY9.
    KOiK12654.
    OMAiLAWSYYI.
    OrthoDBiEOG79GT88.
    PhylomeDBiQ3TBT3.
    TreeFamiTF324444.

    Family and domain databases

    InterProiIPR029158. STING.
    [Graphical view]
    PfamiPF15009. TMEM173. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3TBT3-1) [UniParc]FASTAAdd to Basket

    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

    MPYSNLHPAI PRPRGHRSKY VALIFLVASL MILWVAKDPP NHTLKYLALH    50
    LASHELGLLL KNLCCLAEEL CHVQSRYQGS YWKAVRACLG CPIHCMAMIL 100
    LSSYFYFLQN TADIYLSWMF GLLVLYKSLS MLLGLQSLTP AEVSAVCEEK 150
    KLNVAHGLAW SYYIGYLRLI LPGLQARIRM FNQLHNNMLS GAGSRRLYIL 200
    FPLDCGVPDN LSVVDPNIRF RDMLPQQNID RAGIKNRVYS NSVYEILENG 250
    QPAGVCILEY ATPLQTLFAM SQDAKAGFSR EDRLEQAKLF CRTLEEILED 300
    VPESRNNCRL IVYQEPTDGN SFSLSQEVLR HIRQEEKEEV TMNAPMTSVA 350
    PPPSVLSQEP RLLISGMDQP LPLRTDLI 378
    Length:378
    Mass (Da):42,830
    Last modified:November 25, 2008 - v2
    Checksum:i656ED19097ACE4C8
    GO
    Isoform 2 (identifier: Q3TBT3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MIVESFGASGNPVGPCHFWSLYGVLLGVHWSVLHLGTFRGIRSAGLWLLM

    Note: No experimental confirmation available.

    Show »
    Length:427
    Mass (Da):48,151
    Checksum:iCC362C808C035BE9
    GO
    Isoform 3 (identifier: Q3TBT3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-116: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:337
    Mass (Da):38,036
    Checksum:i9F25E302E7E0FCE8
    GO

    Sequence cautioni

    The sequence BAE42563.1 differs from that shown. Reason: Frameshift at position 377.
    The sequence AAH27757.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC37010.1 differs from that shown. Reason: Erroneous termination at position 203. Translated as Leu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111P → Q in BAE27042. (PubMed:16141072)Curated
    Sequence conflicti39 – 391P → S in BAB27972. (PubMed:16141072)Curated
    Sequence conflicti98 – 981M → V in BAE42563. (PubMed:16141072)Curated
    Sequence conflicti111 – 1111T → N in BAC37010. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101N → D in BAE34068. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101N → D in BAE42310. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101N → D in BAE42224. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101N → D in BAE32222. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101N → D in BAE34517. (PubMed:16141072)Curated
    Sequence conflicti315 – 3151E → K in BAC37010. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MIVESFGASGNPVGPCHFWS LYGVLLGVHWSVLHLGTFRG IRSAGLWLLM in isoform 2. 1 PublicationVSP_022284
    Alternative sequencei76 – 11641Missing in isoform 3. 1 PublicationVSP_022285Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ222242 mRNA. Translation: ACI46649.1.
    DQ910493 mRNA. Translation: ABI78935.1.
    AK012006 mRNA. Translation: BAB27972.1.
    AK077788 mRNA. Translation: BAC37010.1. Sequence problems.
    AK089405 mRNA. Translation: BAC40870.1.
    AK146284 mRNA. Translation: BAE27042.1.
    AK153868 mRNA. Translation: BAE32222.1.
    AK157370 mRNA. Translation: BAE34068.1.
    AK158458 mRNA. Translation: BAE34517.1.
    AK170724 mRNA. Translation: BAE41981.1.
    AK171065 mRNA. Translation: BAE42224.1.
    AK171203 mRNA. Translation: BAE42310.1.
    AK171612 mRNA. Translation: BAE42563.1. Frameshift.
    CH466557 Genomic DNA. Translation: EDK97142.1.
    BC027757 mRNA. Translation: AAH27757.1. Different initiation.
    BC046640 mRNA. Translation: AAH46640.1.
    CCDSiCCDS50253.1. [Q3TBT3-1]
    RefSeqiNP_001276520.1. NM_001289591.1. [Q3TBT3-2]
    NP_001276521.1. NM_001289592.1. [Q3TBT3-3]
    NP_082537.1. NM_028261.1. [Q3TBT3-1]
    XP_006526346.1. XM_006526283.1. [Q3TBT3-1]
    UniGeneiMm.45995.

    Genome annotation databases

    EnsembliENSMUST00000115728; ENSMUSP00000111393; ENSMUSG00000024349. [Q3TBT3-1]
    GeneIDi72512.
    KEGGimmu:72512.
    UCSCiuc008emt.3. mouse. [Q3TBT3-1]
    uc008emu.3. mouse. [Q3TBT3-3]
    uc008emv.3. mouse. [Q3TBT3-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ222242 mRNA. Translation: ACI46649.1 .
    DQ910493 mRNA. Translation: ABI78935.1 .
    AK012006 mRNA. Translation: BAB27972.1 .
    AK077788 mRNA. Translation: BAC37010.1 . Sequence problems.
    AK089405 mRNA. Translation: BAC40870.1 .
    AK146284 mRNA. Translation: BAE27042.1 .
    AK153868 mRNA. Translation: BAE32222.1 .
    AK157370 mRNA. Translation: BAE34068.1 .
    AK158458 mRNA. Translation: BAE34517.1 .
    AK170724 mRNA. Translation: BAE41981.1 .
    AK171065 mRNA. Translation: BAE42224.1 .
    AK171203 mRNA. Translation: BAE42310.1 .
    AK171612 mRNA. Translation: BAE42563.1 . Frameshift.
    CH466557 Genomic DNA. Translation: EDK97142.1 .
    BC027757 mRNA. Translation: AAH27757.1 . Different initiation.
    BC046640 mRNA. Translation: AAH46640.1 .
    CCDSi CCDS50253.1. [Q3TBT3-1 ]
    RefSeqi NP_001276520.1. NM_001289591.1. [Q3TBT3-2 ]
    NP_001276521.1. NM_001289592.1. [Q3TBT3-3 ]
    NP_082537.1. NM_028261.1. [Q3TBT3-1 ]
    XP_006526346.1. XM_006526283.1. [Q3TBT3-1 ]
    UniGenei Mm.45995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JC5 X-ray 2.75 A/B 149-348 [» ]
    4KBY X-ray 2.36 A/B 138-344 [» ]
    4KC0 X-ray 2.20 A/B 138-344 [» ]
    4LOJ X-ray 1.77 A/B 154-340 [» ]
    4LOK X-ray 2.07 A/B 154-340 [» ]
    4LOL X-ray 2.43 A/B 154-340 [» ]
    ProteinModelPortali Q3TBT3.
    SMRi Q3TBT3. Positions 155-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59959N.
    IntActi Q3TBT3. 4 interactions.

    PTM databases

    PhosphoSitei Q3TBT3.

    Proteomic databases

    PaxDbi Q3TBT3.
    PRIDEi Q3TBT3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000115728 ; ENSMUSP00000111393 ; ENSMUSG00000024349 . [Q3TBT3-1 ]
    GeneIDi 72512.
    KEGGi mmu:72512.
    UCSCi uc008emt.3. mouse. [Q3TBT3-1 ]
    uc008emu.3. mouse. [Q3TBT3-3 ]
    uc008emv.3. mouse. [Q3TBT3-2 ]

    Organism-specific databases

    CTDi 340061.
    MGIi MGI:1919762. Tmem173.

    Phylogenomic databases

    eggNOGi NOG43926.
    GeneTreei ENSGT00390000008582.
    HOVERGENi HBG094065.
    InParanoidi A7YGY9.
    KOi K12654.
    OMAi LAWSYYI.
    OrthoDBi EOG79GT88.
    PhylomeDBi Q3TBT3.
    TreeFami TF324444.

    Enzyme and pathway databases

    Reactomei REACT_196447. IRF3-mediated induction of type I IFN.
    REACT_196457. STING mediated induction of host immune responses.
    REACT_196519. Regulation of innate immune responses to cytosolic DNA.
    REACT_198980. IRF3 mediated activation of type 1 IFN.
    REACT_227400. STAT6-mediated induction of chemokines.

    Miscellaneous databases

    NextBioi 336376.
    PROi Q3TBT3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3TBT3.
    CleanExi MM_TMEM173.
    Genevestigatori Q3TBT3.

    Family and domain databases

    InterProi IPR029158. STING.
    [Graphical view ]
    Pfami PF15009. TMEM173. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation."
      Zhong B., Yang Y., Li S., Wang Y.-Y., Li Y., Diao F., Lei C., He X., Zhang L., Tien P., Shu H.-B.
      Immunity 29:538-550(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "MPYS, a novel membrane tetraspanner, is associated with major histocompatibility complex class II and mediates transduction of apoptotic signals."
      Jin L., Waterman P.M., Jonscher K.R., Short C.M., Reisdorph N.A., Cambier J.C.
      Mol. Cell. Biol. 28:5014-5026(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Strain: C57BL/6J.
      Tissue: Embryo, Inner ear, Spleen and Thymus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Strain: Czech II and FVB/N.
      Tissue: Mammary gland.
    6. "STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling."
      Ishikawa H., Barber G.N.
      Nature 455:674-678(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity."
      Ishikawa H., Ma Z., Barber G.N.
      Nature 461:788-792(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    8. "ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization."
      Sun W., Li Y., Chen L., Chen H., You F., Zhou X., Zhou Y., Zhai Z., Chen D., Jiang Z.
      Proc. Natl. Acad. Sci. U.S.A. 106:8653-8658(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger that activates STING."
      Ablasser A., Goldeck M., Cavlar T., Deimling T., Witte G., Rohl I., Hopfner K.P., Ludwig J., Hornung V.
      Nature 498:380-384(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA."
      Wu J., Sun L., Chen X., Du F., Shi H., Chen C., Chen Z.J.
      Science 339:826-830(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CGAMP-BINDING, MUTAGENESIS OF SER-161; TYR-239 AND ASN-241.
    11. "Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING."
      Chin K.H., Tu Z.L., Su Y.C., Yu Y.J., Chen H.C., Lo Y.C., Chen C.P., Barber G.N., Chuah M.L., Liang Z.X., Chou S.H.
      Acta Crystallogr. D 69:352-366(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 138-344 IN COMPLEX WITH CYCLIC DIGUANOSINE MONOPHOSPHATE, SUBUNIT.

    Entry informationi

    Entry nameiSTING_MOUSE
    AccessioniPrimary (citable) accession number: Q3TBT3
    Secondary accession number(s): A7YGY9
    , Q3TAV5, Q3TYP5, Q3TZY8, Q3UJW3, Q8C227, Q8C5Q3, Q8K393, Q9CZY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Was named MPYS because the protein sequence begins by Met-Pro-Tyr-Ser residues.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3