SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q86WV6

- STING_HUMAN

UniProt

Q86WV6 - STING_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Stimulator of interferon genes protein

Gene
TMEM173, ERIS, MITA, STING
Organism
Homo sapiens (Human)
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. 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
Complete GO annotation...

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; 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.6 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei21 – 4121Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini42 – 465Extracellular Reviewed prediction
Transmembranei47 – 6721Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini68 – 8619Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei87 – 10620Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini107 – 1159Extracellular Reviewed prediction
Transmembranei116 – 13621Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini137 – 379243Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi76 – 783RYR → AYA: Abolishes the endoplasmic reticulum location. 1 Publication
Mutagenesisi137 – 1371K → R: Does not affect amount of ubiquitination. 1 Publication
Mutagenesisi150 – 1501K → R: Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta. 2 Publications
Mutagenesisi162 – 1621S → A: Slight decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi166 – 1661G → S: Slight decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi178 – 1803RIR → AIA: Abolishes the endoplasmic reticulum location. 1 Publication
Mutagenesisi240 – 2401Y → S: Strong decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi242 – 2421N → A: Strong decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi260 – 2601E → A: Strong decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi263 – 2631T → A: Strong decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi264 – 2641P → A: Strong decrease in c-di-GMP-binding. 1 Publication
Mutagenesisi267 – 2671T → A: Strong decrease in c-di-GMP-binding. 1 Publication
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. 1 Publication

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)2 Publications
Modified residuei358 – 3581Phosphoserine; by TBK11 Publication

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.2 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 IFIT2.11 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.

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 (1 Publication, 1 Publication, 1 Publication, 1 Publication and 1 Publication).

Sequence similaritiesi

Belongs to the TMEM173 family.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621A → T in BAF83350. 1 Publication
Sequence conflicti363 – 3631L → F in BAF83350. 1 Publication

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

« 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, 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: September 3, 2014
This is version 90 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

Similar proteinsi