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Q86WV6

- STING_HUMAN

UniProt

Q86WV6 - STING_HUMAN

Protein

Stimulator of interferon genes protein

Gene

TMEM173

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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. Essential for the induction of IFN-beta in response to human herpes simplex virus 1 (HHV-1) infection.10 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei263 – 2631c-di-GMP

    GO - Molecular functioni

    1. cyclic-di-GMP binding Source: UniProtKB
    2. cyclic-GMP-AMP binding Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. activation of innate immune response Source: BHF-UCL
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to exogenous dsRNA Source: BHF-UCL
    4. cellular response to interferon-beta Source: Ensembl
    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: BHF-UCL
    9. positive regulation of protein binding Source: BHF-UCL
    10. positive regulation of protein import into nucleus, translocation Source: BHF-UCL
    11. positive regulation of transcription factor import into nucleus Source: BHF-UCL
    12. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    13. positive regulation of type I interferon production Source: Reactome
    14. regulation of type I interferon production Source: Reactome

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_147841. STING mediated induction of host immune responses.
    REACT_163734. STAT6-mediated induction of chemokines.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stimulator of interferon genes protein
    Short name:
    hSTING
    Alternative name(s):
    Endoplasmic reticulum interferon stimulator
    Short name:
    ERIS
    Mediator of IRF3 activation
    Short name:
    hMITA
    Transmembrane protein 173
    Gene namesi
    Name:TMEM173
    Synonyms:ERIS, MITA, STING
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:27962. TMEM173.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201K → R: Does not affect amount of ubiquitination. 2 Publications
    Mutagenesisi76 – 783RYR → AYA: Abolishes the endoplasmic reticulum location. 1 Publication
    Mutagenesisi137 – 1371K → R: Does not affect amount of ubiquitination. 2 Publications
    Mutagenesisi150 – 1501K → R: Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta. 3 Publications
    Mutagenesisi162 – 1621S → A: Slight decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi166 – 1661G → S: Slight decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi178 – 1803RIR → AIA: Abolishes the endoplasmic reticulum location. 1 Publication
    Mutagenesisi240 – 2401Y → S: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi242 – 2421N → A: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi260 – 2601E → A: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi263 – 2631T → A: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi264 – 2641P → A: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi267 – 2671T → A: Strong decrease in c-di-GMP-binding. 2 Publications
    Mutagenesisi324 – 3263SLS → ALA: Induces a decrease in phosphorylation by TBK1. 1 Publication
    Mutagenesisi358 – 3581S → A: Induces a decrease in phosphorylation by TBK1 and ability to activate IRF-E. 2 Publications

    Organism-specific databases

    PharmGKBiPA162405934.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Stimulator of interferon genes proteinPRO_0000271116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki150 – 150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
    Modified residuei358 – 3581Phosphoserine; by TBK12 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues upon MHC-II aggregation By similarity. Phosphorylated on Ser-358 by TBK1, leading to activation and production of IFN-beta.By similarity2 Publications
    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.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ86WV6.
    PaxDbiQ86WV6.
    PRIDEiQ86WV6.

    PTM databases

    PhosphoSiteiQ86WV6.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ86WV6.
    BgeeiQ86WV6.
    CleanExiHS_TMEM173.
    GenevestigatoriQ86WV6.

    Organism-specific databases

    HPAiHPA038534.

    Interactioni

    Subunit structurei

    Associates with the MHC-II complex By similarity. Homodimer; 'Lys-63'-linked ubiquitination at Lys-150 is required for homodimerization. Interacts with DDX58/RIG-I, MAVS and SSR2. Interacts with RNF5 and TRIM56. Interacts with TBK1; when homodimer, leading to subsequent production of IFN-beta. Interacts with IFIT1 and IFIT2.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2800345,EBI-2800345
    P279585EBI-2800345,EBI-8763498From a different organism.
    Q99IB85EBI-2800345,EBI-6928570From a different organism.
    CCDC47Q96A332EBI-2800345,EBI-720151
    DDOSTP396562EBI-2800345,EBI-358866
    IFI16Q166662EBI-2800345,EBI-2867186
    IRAK1P516172EBI-2800345,EBI-358664
    LTN1O948222EBI-2800345,EBI-1044684
    MAVSQ7Z4347EBI-2800345,EBI-995373
    MBOAT7Q96N662EBI-2800345,EBI-6116499
    SGPL1O954702EBI-2800345,EBI-1046170
    STAT6P4222612EBI-2800345,EBI-1186478
    STT3AP469772EBI-2800345,EBI-719212
    SURF4O152602EBI-2800345,EBI-1044848
    TBK1Q9UHD23EBI-2800345,EBI-356402

    Protein-protein interaction databases

    BioGridi130988. 31 interactions.
    DIPiDIP-48847N.
    IntActiQ86WV6. 29 interactions.
    STRINGi9606.ENSP00000331288.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi156 – 16611
    Helixi168 – 18518
    Turni186 – 1894
    Beta strandi196 – 2038
    Helixi212 – 2154
    Beta strandi219 – 2257
    Beta strandi228 – 2325
    Beta strandi235 – 2406
    Beta strandi242 – 2498
    Beta strandi252 – 26110
    Helixi264 – 2729
    Helixi275 – 2773
    Helixi281 – 30121
    Helixi303 – 3064
    Beta strandi309 – 3146
    Beta strandi318 – 3203
    Helixi325 – 3339
    Turni334 – 3363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EF4X-ray2.15A/B139-379[»]
    4EF5X-ray2.45A139-379[»]
    4EMTX-ray1.50A/B155-341[»]
    4EMUX-ray1.90A/B155-341[»]
    4F5DX-ray3.00A/B141-379[»]
    4F5EX-ray2.60A141-379[»]
    4F5WX-ray2.20A149-379[»]
    4F5YX-ray2.40A/B149-379[»]
    4F9EX-ray2.75A139-379[»]
    4F9GX-ray2.95A/C139-379[»]
    4KSYX-ray1.88A138-379[»]
    4LOHX-ray2.25A/B155-341[»]
    4LOIX-ray1.89A/B155-341[»]
    ProteinModelPortaliQ86WV6.
    SMRiQ86WV6. Positions 151-343.
    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 – 1159ExtracellularSequence Analysis
    Topological domaini137 – 379243CytoplasmicSequence 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
    Transmembranei116 – 13621Helical; Name=4Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni153 – 340188c-di-GMP-binding domain (CBD)Add
    BLAST
    Regioni162 – 1676c-di-GMP binding
    Regioni238 – 2414c-di-GMP binding
    Regioni340 – 37940C-terminal tail (CTT)Add
    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 (PubMed:22579474, PubMed:22705373, PubMed:22728658, PubMed:22728660 and PubMed:22728659).

    Sequence similaritiesi

    Belongs to the TMEM173 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43926.
    HOGENOMiHOG000076316.
    HOVERGENiHBG094065.
    InParanoidiQ86WV6.
    KOiK12654.
    OMAiLAWSYYI.
    OrthoDBiEOG79GT88.
    PhylomeDBiQ86WV6.
    TreeFamiTF324444.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q86WV6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHSSLHPSI PCPRGHGAQK AALVLLSACL VTLWGLGEPP EHTLRYLVLH    50
    LASLQLGLLL NGVCSLAEEL RHIHSRYRGS YWRTVRACLG CPLRRGALLL 100
    LSIYFYYSLP NAVGPPFTWM LALLGLSQAL NILLGLKGLA PAEISAVCEK 150
    GNFNVAHGLA WSYYIGYLRL ILPELQARIR TYNQHYNNLL RGAVSQRLYI 200
    LLPLDCGVPD NLSMADPNIR FLDKLPQQTG DHAGIKDRVY SNSIYELLEN 250
    GQRAGTCVLE YATPLQTLFA MSQYSQAGFS REDRLEQAKL FCRTLEDILA 300
    DAPESQNNCR LIAYQEPADD SSFSLSQEVL RHLRQEEKEE VTVGSLKTSA 350
    VPSTSTMSQE PELLISGMEK PLPLRTDFS 379
    Length:379
    Mass (Da):42,193
    Last modified:June 1, 2003 - v1
    Checksum:iCB54D6A4D4D8E7C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2621A → T in BAF83350. (PubMed:14702039)Curated
    Sequence conflicti363 – 3631L → F in BAF83350. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711R → H.
    Corresponds to variant rs11554776 [ dbSNP | Ensembl ].
    VAR_029863
    Natural varianti232 – 2321H → R.1 Publication
    Corresponds to variant rs1131769 [ dbSNP | Ensembl ].
    VAR_029864
    Natural varianti293 – 2931R → Q.
    Corresponds to variant rs7380824 [ dbSNP | Ensembl ].
    VAR_029865

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ222241 mRNA. Translation: ACI46648.1.
    AK290661 mRNA. Translation: BAF83350.1.
    AC138517 Genomic DNA. No translation available.
    BC047779 mRNA. Translation: AAH47779.1.
    CCDSiCCDS4215.1.
    RefSeqiNP_938023.1. NM_198282.2.
    UniGeneiHs.379754.

    Genome annotation databases

    EnsembliENST00000330794; ENSP00000331288; ENSG00000184584.
    GeneIDi340061.
    KEGGihsa:340061.
    UCSCiuc003lep.3. human.

    Polymorphism databases

    DMDMi74727720.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ222241 mRNA. Translation: ACI46648.1 .
    AK290661 mRNA. Translation: BAF83350.1 .
    AC138517 Genomic DNA. No translation available.
    BC047779 mRNA. Translation: AAH47779.1 .
    CCDSi CCDS4215.1.
    RefSeqi NP_938023.1. NM_198282.2.
    UniGenei Hs.379754.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EF4 X-ray 2.15 A/B 139-379 [» ]
    4EF5 X-ray 2.45 A 139-379 [» ]
    4EMT X-ray 1.50 A/B 155-341 [» ]
    4EMU X-ray 1.90 A/B 155-341 [» ]
    4F5D X-ray 3.00 A/B 141-379 [» ]
    4F5E X-ray 2.60 A 141-379 [» ]
    4F5W X-ray 2.20 A 149-379 [» ]
    4F5Y X-ray 2.40 A/B 149-379 [» ]
    4F9E X-ray 2.75 A 139-379 [» ]
    4F9G X-ray 2.95 A/C 139-379 [» ]
    4KSY X-ray 1.88 A 138-379 [» ]
    4LOH X-ray 2.25 A/B 155-341 [» ]
    4LOI X-ray 1.89 A/B 155-341 [» ]
    ProteinModelPortali Q86WV6.
    SMRi Q86WV6. Positions 151-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130988. 31 interactions.
    DIPi DIP-48847N.
    IntActi Q86WV6. 29 interactions.
    STRINGi 9606.ENSP00000331288.

    PTM databases

    PhosphoSitei Q86WV6.

    Polymorphism databases

    DMDMi 74727720.

    Proteomic databases

    MaxQBi Q86WV6.
    PaxDbi Q86WV6.
    PRIDEi Q86WV6.

    Protocols and materials databases

    DNASUi 340061.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330794 ; ENSP00000331288 ; ENSG00000184584 .
    GeneIDi 340061.
    KEGGi hsa:340061.
    UCSCi uc003lep.3. human.

    Organism-specific databases

    CTDi 340061.
    GeneCardsi GC05M138836.
    HGNCi HGNC:27962. TMEM173.
    HPAi HPA038534.
    MIMi 612374. gene.
    neXtProti NX_Q86WV6.
    PharmGKBi PA162405934.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43926.
    HOGENOMi HOG000076316.
    HOVERGENi HBG094065.
    InParanoidi Q86WV6.
    KOi K12654.
    OMAi LAWSYYI.
    OrthoDBi EOG79GT88.
    PhylomeDBi Q86WV6.
    TreeFami TF324444.

    Enzyme and pathway databases

    Reactomei REACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_147841. STING mediated induction of host immune responses.
    REACT_163734. STAT6-mediated induction of chemokines.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.

    Miscellaneous databases

    GenomeRNAii 340061.
    NextBioi 97672.
    PROi Q86WV6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86WV6.
    Bgeei Q86WV6.
    CleanExi HS_TMEM173.
    Genevestigatori Q86WV6.

    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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MAVS, PHOSPHORYLATION AT SER-358, MUTAGENESIS OF 324-SER--SER-326 AND SER-358.
    2. "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], VARIANT ARG-232.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    5. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DDX58 AND SSR2.
    6. "The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA."
      Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y., Zhang X.L., Shu H.B.
      Immunity 30:397-407(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-150, INTERACTION WITH RNF5, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-150.
    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.
    8. "ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response."
      Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y., Yang F., Shu H.B.
      Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT1; IFIT2; MAVS AND TBK1.
    9. "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, SUBCELLULAR LOCATION, HOMODIMERIZATION, PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF 76-ARG--ARG-78 AND 178-ARG--ARG-180.
    10. "The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA."
      Tsuchida T., Zou J., Saitoh T., Kumar H., Abe T., Matsuura Y., Kawai T., Akira S.
      Immunity 33:765-776(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, UBIQUITINATION AT LYS-150, MUTAGENESIS OF LYS-20; LYS-137 AND LYS-150.
    11. Cited for: FUNCTION, C-DI-GMP-BINDING.
    12. "Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein."
      Orzalli M.H., DeLuca N.A., Knipe D.M.
      Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "The innate immune DNA sensor cGAS produces a noncanonical cyclic dinucleotide that activates human STING."
      Diner E.J., Burdette D.L., Wilson S.C., Monroe K.M., Kellenberger C.A., Hyodo M., Hayakawa Y., Hammond M.C., Vance R.E.
      Cell Rep. 3:1355-1361(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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.
    15. "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.
    16. "Structural analysis of the STING adaptor protein reveals a hydrophobic dimer interface and mode of cyclic di-GMP binding."
      Ouyang S., Song X., Wang Y., Ru H., Shaw N., Jiang Y., Niu F., Zhu Y., Qiu W., Parvatiyar K., Li Y., Zhang R., Cheng G., Liu Z.J.
      Immunity 36:1073-1086(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 139-379, SUBUNIT, C-DI-GMP-BINDING.
    17. "Cyclic di-GMP sensing via the innate immune signaling protein STING."
      Yin Q., Tian Y., Kabaleeswaran V., Jiang X., Tu D., Eck M.J., Chen Z.J., Wu H.
      Mol. Cell 46:735-745(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 139-379, SUBUNIT, C-DI-GMP-BINDING.
    18. "Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system."
      Shu C., Yi G., Watts T., Kao C.C., Li P.
      Nat. Struct. Mol. Biol. 19:722-724(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 155-341, SUBUNIT, C-DI-GMP-BINDING, MUTAGENESIS OF SER-162; GLY-166; TYR-240; ASN-242; GLU-260; THR-263; PRO-264 AND THR-267.
    19. "Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP."
      Shang G., Zhu D., Li N., Zhang J., Zhu C., Lu D., Liu C., Yu Q., Zhao Y., Xu S., Gu L.
      Nat. Struct. Mol. Biol. 19:725-727(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 149-379, SUBUNIT, C-DI-GMP-BINDING.
    20. "The structural basis for the sensing and binding of cyclic di-GMP by STING."
      Huang Y.H., Liu X.Y., Du X.X., Jiang Z.F., Su X.D.
      Nat. Struct. Mol. Biol. 19:728-730(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 141-379, SUBUNIT, C-DI-GMP-BINDING.

    Entry informationi

    Entry nameiSTING_HUMAN
    AccessioniPrimary (citable) accession number: Q86WV6
    Secondary accession number(s): A8K3P6
    , B6EB35, D6RBX0, D6RE01, D6RID9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 91 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3