Q86WV6 (STING_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TMEM173
Synonyms:	ERIS, MITA, STING

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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.13 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity. Cytoplasm › perinuclear 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.13, Ref.14, Ref.15, Ref.16 and Ref.17).
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 process	Apoptosis Immunity Innate immunity
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Nucleotide-binding
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation 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: Compara 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
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from direct assay Ref.9. Source: UniProtKB integral to 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 plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cyclic-GMP-AMP binding Inferred from sequence or structural similarity. Source: UniProtKB cyclic-di-GMP binding Inferred from direct assay Ref.14. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.9Ref.10Ref.14. Source: UniProtKB protein kinase binding Inferred from direct assay Ref.1. Source: BHF-UCL transcription factor binding Inferred from direct assay Ref.1. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCDC47	Q96A33	2	EBI-2800345,EBI-720151
DDOST	P39656	2	EBI-2800345,EBI-358866
IFI16	Q16666	2	EBI-2800345,EBI-2867186
IRAK1	P51617	2	EBI-2800345,EBI-358664
LTN1	O94822	2	EBI-2800345,EBI-1044684
MBOAT7	Q96N66	2	EBI-2800345,EBI-6116499
SGPL1	O95470	2	EBI-2800345,EBI-1046170
STAT6	P42226	12	EBI-2800345,EBI-1186478
STT3A	P46977	2	EBI-2800345,EBI-719212
SURF4	O15260	2	EBI-2800345,EBI-1044848

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Stimulator of interferon genes protein

PRO_0000271116

Regions

Topological domain

1 – 20

20

Cytoplasmic Potential

Transmembrane

21 – 41

21

Helical; Name=1; Potential

Topological domain

42 – 46

5

Extracellular Potential

Transmembrane

47 – 67

21

Helical; Name=2; Potential

Topological domain

68 – 86

19

Cytoplasmic Potential

Transmembrane

87 – 106

20

Helical; Name=3; Potential

Topological domain

107 – 115

9

Extracellular Potential

Transmembrane

116 – 136

21

Helical; Name=4; Potential

Topological domain

137 – 379

243

Cytoplasmic Potential

Region

153 – 340

188

c-di-GMP-binding domain (CBD)

Region

340 – 379

40

C-terminal tail (CTT)

Sites

Binding site

263

1

c-di-GMP

Site

167

1

Required for c-di-GMP-binding

Amino acid modifications

Modified residue

358

1

Phosphoserine; by TBK1 Ref.1

Cross-link

150

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.10

Natural variations

Natural variant

71

1

R → H.
Corresponds to variant rs11554776 [ dbSNP | Ensembl ].

VAR_029863

Natural variant

232

1

H → R. Ref.2
Corresponds to variant rs1131769 [ dbSNP | Ensembl ].

VAR_029864

Natural variant

293

1

R → Q.
Corresponds to variant rs7380824 [ dbSNP | Ensembl ].

VAR_029865

Experimental info

Mutagenesis

20

1

K → R: Does not affect amount of ubiquitination. Ref.10

Mutagenesis

76 – 78

3

RYR → AYA: Abolishes the endoplasmic reticulum location. Ref.9

Mutagenesis

137

1

K → R: Does not affect amount of ubiquitination. Ref.10

Mutagenesis

150

1

K → R: Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta. Ref.6 Ref.10

Mutagenesis

162

1

S → A: Slight decrease in c-di-GMP-binding. Ref.15

Mutagenesis

166

1

G → S: Slight decrease in c-di-GMP-binding. Ref.15

Mutagenesis

178 – 180

3

RIR → AIA: Abolishes the endoplasmic reticulum location. Ref.9

Mutagenesis

240

1

Y → S: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

242

1

N → A: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

260

1

E → A: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

263

1

T → A: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

264

1

P → A: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

267

1

T → A: Strong decrease in c-di-GMP-binding. Ref.15

Mutagenesis

324 – 326

3

SLS → ALA: Induces a decrease in phosphorylation by TBK1. Ref.1

Mutagenesis

358

1

S → A: Induces a decrease in phosphorylation by TBK1 and ability to activate IRF-E. Ref.1

Sequence conflict

262

1

A → T in BAF83350. Ref.2

Sequence conflict

363

1

L → F in BAF83350. Ref.2

Secondary structure

1

.

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379

Helix Strand Turn

Details...

Helix

156 – 166

11

Helix

168 – 185

18

Turn

186 – 189

4

Beta strand

196 – 203

8

Helix

212 – 215

4

Beta strand

219 – 225

7

Beta strand

233 – 235

3

Beta strand

242 – 249

8

Beta strand

252 – 261

10

Helix

264 – 272

9

Helix

275 – 277

3

Helix

281 – 301

21

Helix

303 – 306

4

Beta strand

309 – 314

6

Beta strand

318 – 320

3

Helix

325 – 333

9

Turn

334 – 336

3

Sequences

	Sequence		Length	Mass (Da)
	Q86WV6 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: CB54D6A4D4D8E7C0	FASTA	379	42,193
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.

IPI

IPI00257059.

RefSeq

NP_938023.1. NM_198282.2.

UniGene

Hs.379754.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q86WV6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48847N.

IntAct

Q86WV6. 26 interactions.

STRING

9606.ENSP00000331288.

PTM databases

PhosphoSite

Q86WV6.

Polymorphism databases

DMDM

74727720.

Proteomic databases

PaxDb

Q86WV6.

PRIDE

Q86WV6.

Protocols and materials databases

DNASU

340061.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330794; ENSP00000331288; ENSG00000184584.

GeneID

340061.

KEGG

hsa:340061.

UCSC

uc003lep.3. human.

Organism-specific databases

CTD

340061.

GeneCards

GC05M138836.

HGNC

HGNC:27962. TMEM173.

HPA

HPA038534.

MIM

612374. gene.

neXtProt

NX_Q86WV6.

PharmGKB

PA162405934.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43926.

HOGENOM

HOG000076316.

HOVERGEN

HBG094065.

InParanoid

Q86WV6.

KO

K12654.

OMA

LFAMSQD.

OrthoDB

EOG4PK295.

PhylomeDB

Q86WV6.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

Q86WV6.

CleanEx

HS_TMEM173.

Genevestigator

Q86WV6.

Family and domain databases

ProtoNet

Search...

Other

GenomeRNAi

340061.

NextBio

97672.

SOURCE

Search...

Entry information

Entry name

STING_HUMAN

Accession

Primary (citable) accession number: Q86WV6
Secondary accession number(s): A8K3P6 , B6EB35, D6RBX0, D6RE01, D6RID9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.