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Q3TBT3

- STING_MOUSE

UniProt

Q3TBT3 - STING_MOUSE

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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

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 homodimerization activity Source: UniProtKB
  4. 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
Complete GO annotation...

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-KW
  6. perinuclear region of cytoplasm Source: UniProtKB
  7. peroxisome Source: MGI
  8. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

MaxQBiQ3TBT3.
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.
InParanoidiQ3TBT3.
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

        10         20         30         40         50
MPYSNLHPAI PRPRGHRSKY VALIFLVASL MILWVAKDPP NHTLKYLALH
60 70 80 90 100
LASHELGLLL KNLCCLAEEL CHVQSRYQGS YWKAVRACLG CPIHCMAMIL
110 120 130 140 150
LSSYFYFLQN TADIYLSWMF GLLVLYKSLS MLLGLQSLTP AEVSAVCEEK
160 170 180 190 200
KLNVAHGLAW SYYIGYLRLI LPGLQARIRM FNQLHNNMLS GAGSRRLYIL
210 220 230 240 250
FPLDCGVPDN LSVVDPNIRF RDMLPQQNID RAGIKNRVYS NSVYEILENG
260 270 280 290 300
QPAGVCILEY ATPLQTLFAM SQDAKAGFSR EDRLEQAKLF CRTLEEILED
310 320 330 340 350
VPESRNNCRL IVYQEPTDGN SFSLSQEVLR HIRQEEKEEV TMNAPMTSVA
360 370
PPPSVLSQEP RLLISGMDQP LPLRTDLI
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

MaxQBi Q3TBT3.
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 Q3TBT3.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 82 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