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Q86WV6 (STING_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TMEM173
Synonyms:ERIS, MITA, STING
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity. Cytoplasmperinuclear region. Note: In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited. Ref.1 Ref.5 Ref.6 Ref.7 Ref.9

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.5

Domain

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 (Ref.15, Ref.16, Ref.17, Ref.18 and Ref.19).

Post-translational modification

Phosphorylated on tyrosine residues upon MHC-II aggregation By similarity. Phosphorylated on Ser-358 by TBK1, leading to activation and production of IFN-beta. Ref.1 Ref.9

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. Ref.6 Ref.9 Ref.10

Sequence similarities

Belongs to the TMEM173 family.

Ontologies

Keywords
   Biological processApoptosis
Immunity
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandNucleotide-binding
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of innate immune response

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to exogenous dsRNA

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

cellular response to interferon-beta

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from direct assay Ref.10. Source: UniProtKB

innate immune response

Inferred from direct assay Ref.10. Source: UniProtKB

interferon-beta production

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of protein binding

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of protein import into nucleus, translocation

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of transcription factor import into nucleus

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of type I interferon production

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from direct assay Ref.9. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from direct assay Ref.1. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclic-GMP-AMP binding

Inferred from sequence or structural similarity. Source: UniProtKB

cyclic-di-GMP binding

Inferred from direct assay Ref.16. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 23542348. Source: IntAct

protein homodimerization activity

Inferred from direct assay Ref.9Ref.10Ref.16. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Stimulator of interferon genes protein
PRO_0000271116

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Name=1; Potential
Topological domain42 – 465Extracellular Potential
Transmembrane47 – 6721Helical; Name=2; Potential
Topological domain68 – 8619Cytoplasmic Potential
Transmembrane87 – 10620Helical; Name=3; Potential
Topological domain107 – 1159Extracellular Potential
Transmembrane116 – 13621Helical; Name=4; Potential
Topological domain137 – 379243Cytoplasmic Potential
Region153 – 340188c-di-GMP-binding domain (CBD)
Region162 – 1676c-di-GMP binding
Region238 – 2414c-di-GMP binding
Region340 – 37940C-terminal tail (CTT)

Sites

Binding site2631c-di-GMP

Amino acid modifications

Modified residue3581Phosphoserine; by TBK1 Ref.1
Cross-link150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.10

Natural variations

Natural variant711R → H.
Corresponds to variant rs11554776 [ dbSNP | Ensembl ].
VAR_029863
Natural variant2321H → R. Ref.2
Corresponds to variant rs1131769 [ dbSNP | Ensembl ].
VAR_029864
Natural variant2931R → Q.
Corresponds to variant rs7380824 [ dbSNP | Ensembl ].
VAR_029865

Experimental info

Mutagenesis201K → R: Does not affect amount of ubiquitination. Ref.10
Mutagenesis76 – 783RYR → AYA: Abolishes the endoplasmic reticulum location. Ref.9
Mutagenesis1371K → R: Does not affect amount of ubiquitination. Ref.10
Mutagenesis1501K → R: Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta. Ref.6 Ref.10
Mutagenesis1621S → A: Slight decrease in c-di-GMP-binding. Ref.17
Mutagenesis1661G → S: Slight decrease in c-di-GMP-binding. Ref.17
Mutagenesis178 – 1803RIR → AIA: Abolishes the endoplasmic reticulum location. Ref.9
Mutagenesis2401Y → S: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis2421N → A: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis2601E → A: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis2631T → A: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis2641P → A: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis2671T → A: Strong decrease in c-di-GMP-binding. Ref.17
Mutagenesis324 – 3263SLS → ALA: Induces a decrease in phosphorylation by TBK1. Ref.1
Mutagenesis3581S → A: Induces a decrease in phosphorylation by TBK1 and ability to activate IRF-E. Ref.1
Sequence conflict2621A → T in BAF83350. Ref.2
Sequence conflict3631L → F in BAF83350. Ref.2

Secondary structure

................................... 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q86WV6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CB54D6A4D4D8E7C0

FASTA37942,193
        10         20         30         40         50         60 
MPHSSLHPSI PCPRGHGAQK AALVLLSACL VTLWGLGEPP EHTLRYLVLH LASLQLGLLL 

        70         80         90        100        110        120 
NGVCSLAEEL RHIHSRYRGS YWRTVRACLG CPLRRGALLL LSIYFYYSLP NAVGPPFTWM 

       130        140        150        160        170        180 
LALLGLSQAL NILLGLKGLA PAEISAVCEK GNFNVAHGLA WSYYIGYLRL ILPELQARIR 

       190        200        210        220        230        240 
TYNQHYNNLL RGAVSQRLYI LLPLDCGVPD NLSMADPNIR FLDKLPQQTG DHAGIKDRVY 

       250        260        270        280        290        300 
SNSIYELLEN GQRAGTCVLE YATPLQTLFA MSQYSQAGFS REDRLEQAKL FCRTLEDILA 

       310        320        330        340        350        360 
DAPESQNNCR LIAYQEPADD SSFSLSQEVL RHLRQEEKEE VTVGSLKTSA VPSTSTMSQE 

       370 
PELLISGMEK PLPLRTDFS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"STING is a direct innate immune sensor of cyclic di-GMP."
Burdette D.L., Monroe K.M., Sotelo-Troha K., Iwig J.S., Eckert B., Hyodo M., Hayakawa Y., Vance R.E.
Nature 478:515-518(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, C-DI-GMP-BINDING.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ222241 mRNA. Translation: ACI46648.1.
AK290661 mRNA. Translation: BAF83350.1.
AC138517 Genomic DNA. No translation available.
BC047779 mRNA. Translation: AAH47779.1.
RefSeqNP_938023.1. NM_198282.2.
UniGeneHs.379754.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ86WV6.
SMRQ86WV6. Positions 151-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130988. 29 interactions.
DIPDIP-48847N.
IntActQ86WV6. 29 interactions.
STRING9606.ENSP00000331288.

PTM databases

PhosphoSiteQ86WV6.

Polymorphism databases

DMDM74727720.

Proteomic databases

PaxDbQ86WV6.
PRIDEQ86WV6.

Protocols and materials databases

DNASU340061.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330794; ENSP00000331288; ENSG00000184584.
GeneID340061.
KEGGhsa:340061.
UCSCuc003lep.3. human.

Organism-specific databases

CTD340061.
GeneCardsGC05M138836.
HGNCHGNC:27962. TMEM173.
HPAHPA038534.
MIM612374. gene.
neXtProtNX_Q86WV6.
PharmGKBPA162405934.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43926.
HOGENOMHOG000076316.
HOVERGENHBG094065.
InParanoidQ86WV6.
KOK12654.
OMALFAMSQD.
OrthoDBEOG79GT88.
PhylomeDBQ86WV6.
TreeFamTF324444.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ86WV6.
BgeeQ86WV6.
CleanExHS_TMEM173.
GenevestigatorQ86WV6.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi340061.
NextBio97672.
PROQ86WV6.
SOURCESearch...

Entry information

Entry nameSTING_HUMAN
AccessionPrimary (citable) accession number: Q86WV6
Secondary accession number(s): A8K3P6 expand/collapse secondary AC list , B6EB35, D6RBX0, D6RE01, D6RID9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM