Q3TBT3 (STING_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Tmem173
Synonyms:	Eris Mita, Mpys, Sting

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	378 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.2 Ref.6 Ref.7 Ref.8 Ref.9
Subunit structure	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. Ref.2
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein. Cytoplasm › perinuclear region. Note: In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited. Ref.2 Ref.7
Tissue specificity	Present in spleen and thymus tissue. Also present in dendritic cells (at protein level). Ref.2
Developmental stage	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. Ref.2
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 By similarity.
Post-translational modification	Phosphorylated on Ser-357 by TBK1, leading to activation and production of IFN-beta By similarity. Phosphorylated on tyrosine residues upon MHC-II aggregation. Ref.2 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.
Disruption phenotype	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. Ref.7
Miscellaneous	Was named MPYS because the protein sequence begins by Met-Pro-Tyr-Ser residues (Ref.2).
Sequence similarities	Belongs to the TMEM173 family.
Sequence caution	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. The sequence BAE42563.1 differs from that shown. Reason: Frameshift at position 377.

Ontologies

Keywords
Biological process	Apoptosis Immunity Innate immunity
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
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 PubMed 21947006Ref.9. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to exogenous dsRNA Inferred from electronic annotation. Source: Compara cellular response to interferon-beta Inferred from mutant phenotype PubMed 21892174. Source: MGI defense response to virus Inferred from mutant phenotype Ref.7. Source: UniProtKB innate immune response Inferred from mutant phenotype Ref.8Ref.7. Source: UniProtKB interferon-beta production Inferred from mutant phenotype Ref.8Ref.7. Source: UniProtKB positive regulation of defense response to virus by host Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from electronic annotation. Source: Compara positive regulation of protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara positive regulation of transcription factor import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 21892174. Source: MGI
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 19926846. Source: MGI endoplasmic reticulum membrane Inferred from direct assay Ref.7. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB peroxisome Inferred from direct assay PubMed 22745163. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cyclic-GMP-AMP binding Inferred from direct assay Ref.9. Source: UniProtKB cyclic-di-GMP binding Inferred from direct assay PubMed 21947006. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3TBT3-1)

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.

Isoform 2 (identifier: Q3TBT3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MIVESFGASGNPVGPCHFWSLYGVLLGVHWSVLHLGTFRGIRSAGLWLLM

Note: No experimental confirmation available.

Isoform 3 (identifier: Q3TBT3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     76-116: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 378

378

Stimulator of interferon genes protein

PRO_0000271117

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 – 114

8

Extracellular Potential

Transmembrane

115 – 135

21

Helical; Name=4; Potential

Topological domain

136 – 378

243

Cytoplasmic Potential

Region

152 – 339

188

c-di-GMP-binding domain (CBD) By similarity

Region

339 – 378

40

C-terminal tail (CTT) By similarity

Sites

Binding site

262

1

c-di-GMP By similarity

Site

166

1

Required for c-di-GMP-binding By similarity

Amino acid modifications

Modified residue

357

1

Phosphoserine; by TBK1 By similarity

Cross-link

150

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence

1

1

M → MIVESFGASGNPVGPCHFWS LYGVLLGVHWSVLHLGTFRG IRSAGLWLLM in isoform 2.

VSP_022284

Alternative sequence

76 – 116

41

Missing in isoform 3.

VSP_022285

Experimental info

Mutagenesis

161

1

S → A: Decrease in cGAMP-binding. Ref.9

Mutagenesis

239

1

Y → S: Strong decrease in cGAMP-binding. Ref.9

Mutagenesis

241

1

N → A: Strong decrease in cGAMP-binding. Ref.9

Sequence conflict

11

1

P → Q in BAE27042. Ref.3

Sequence conflict

39

1

P → S in BAB27972. Ref.3

Sequence conflict

98

1

M → V in BAE42563. Ref.3

Sequence conflict

111

1

T → N in BAC37010. Ref.3

Sequence conflict

210

1

N → D in BAE34068. Ref.3

Sequence conflict

210

1

N → D in BAE42310. Ref.3

Sequence conflict

210

1

N → D in BAE42224. Ref.3

Sequence conflict

210

1

N → D in BAE32222. Ref.3

Sequence conflict

210

1

N → D in BAE34517. Ref.3

Sequence conflict

315

1

E → K in BAC37010. Ref.3

Secondary structure

1

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378

Helix Strand Turn

Details...

Helix

156 – 164

9

Helix

167 – 170

4

Helix

171 – 173

3

Helix

174 – 184

11

Turn

185 – 187

3

Beta strand

194 – 202

9

Beta strand

209 – 212

4

Beta strand

218 – 223

6

Beta strand

228 – 230

3

Beta strand

242 – 248

7

Beta strand

251 – 260

10

Helix

263 – 270

8

Helix

284 – 299

16

Beta strand

301 – 303

3

Beta strand

307 – 313

7

Beta strand

317 – 320

4

Helix

324 – 333

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 656ED19097ACE4C8	FASTA	378	42,830
	10 20 30 40 50 60 MPYSNLHPAI PRPRGHRSKY VALIFLVASL MILWVAKDPP NHTLKYLALH LASHELGLLL 70 80 90 100 110 120 KNLCCLAEEL CHVQSRYQGS YWKAVRACLG CPIHCMAMIL LSSYFYFLQN TADIYLSWMF 130 140 150 160 170 180 GLLVLYKSLS MLLGLQSLTP AEVSAVCEEK KLNVAHGLAW SYYIGYLRLI LPGLQARIRM 190 200 210 220 230 240 FNQLHNNMLS GAGSRRLYIL FPLDCGVPDN LSVVDPNIRF RDMLPQQNID RAGIKNRVYS 250 260 270 280 290 300 NSVYEILENG QPAGVCILEY ATPLQTLFAM SQDAKAGFSR EDRLEQAKLF CRTLEEILED 310 320 330 340 350 360 VPESRNNCRL IVYQEPTDGN SFSLSQEVLR HIRQEEKEEV TMNAPMTSVA PPPSVLSQEP 370 RLLISGMDQP LPLRTDLI
	Isoform 2 [UniParc]. Checksum: CC362C808C035BE9	FASTA	427	48,151
	10 20 30 40 50 60 MIVESFGASG NPVGPCHFWS LYGVLLGVHW SVLHLGTFRG IRSAGLWLLM PYSNLHPAIP 70 80 90 100 110 120 RPRGHRSKYV ALIFLVASLM ILWVAKDPPN HTLKYLALHL ASHELGLLLK NLCCLAEELC 130 140 150 160 170 180 HVQSRYQGSY WKAVRACLGC PIHCMAMILL SSYFYFLQNT ADIYLSWMFG LLVLYKSLSM 190 200 210 220 230 240 LLGLQSLTPA EVSAVCEEKK LNVAHGLAWS YYIGYLRLIL PGLQARIRMF NQLHNNMLSG 250 260 270 280 290 300 AGSRRLYILF PLDCGVPDNL SVVDPNIRFR DMLPQQNIDR AGIKNRVYSN SVYEILENGQ 310 320 330 340 350 360 PAGVCILEYA TPLQTLFAMS QDAKAGFSRE DRLEQAKLFC RTLEEILEDV PESRNNCRLI 370 380 390 400 410 420 VYQEPTDGNS FSLSQEVLRH IRQEEKEEVT MNAPMTSVAP PPSVLSQEPR LLISGMDQPL PLRTDLI
	Isoform 3 [UniParc]. Checksum: 9F25E302E7E0FCE8	FASTA	337	38,036
	10 20 30 40 50 60 MPYSNLHPAI PRPRGHRSKY VALIFLVASL MILWVAKDPP NHTLKYLALH LASHELGLLL 70 80 90 100 110 120 KNLCCLAEEL CHVQSSWMFG LLVLYKSLSM LLGLQSLTPA EVSAVCEEKK LNVAHGLAWS 130 140 150 160 170 180 YYIGYLRLIL PGLQARIRMF NQLHNNMLSG AGSRRLYILF PLDCGVPDNL SVVDPNIRFR 190 200 210 220 230 240 DMLPQQNIDR AGIKNRVYSN SVYEILENGQ PAGVCILEYA TPLQTLFAMS QDAKAGFSRE 250 260 270 280 290 300 DRLEQAKLFC RTLEEILEDV PESRNNCRLI VYQEPTDGNS FSLSQEVLRH IRQEEKEEVT 310 320 330 MNAPMTSVAP PPSVLSQEPR LLISGMDQPL PLRTDLI

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.
[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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00651829.
IPI00674006.
IPI00677447.

RefSeq

NP_082537.1. NM_028261.1.

UniGene

Mm.45995.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4G3L	X-ray	2.40	A/B	138-344	[»]
4G4D	X-ray	2.40	A/B	138-344	[»]

ProteinModelPortal

Q3TBT3.

SMR

Q3TBT3. Positions 152-342.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59959N.

IntAct

Q3TBT3. 4 interactions.

PTM databases

PhosphoSite

Q3TBT3.

Proteomic databases

PaxDb

Q3TBT3.

PRIDE

Q3TBT3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000115728; ENSMUSP00000111393; ENSMUSG00000024349.

GeneID

72512.

KEGG

mmu:72512.

UCSC

uc008emt.3. mouse.
uc008emu.3. mouse.
uc008emv.3. mouse.

Organism-specific databases

CTD

340061.

MGI

MGI:1919762. Tmem173.

Phylogenomic databases

eggNOG

NOG43926.

GeneTree

ENSGT00390000008582.

HOVERGEN

HBG094065.

InParanoid

A7YGY9.

KO

K12654.

OMA

LFAMSQD.

OrthoDB

EOG4PK295.

Gene expression databases

Bgee

Q3TBT3.

CleanEx

MM_TMEM173.

Genevestigator

Q3TBT3.

Family and domain databases

ProtoNet

Search...

Other

NextBio

336376.

SOURCE

Search...

Entry information

Entry name

STING_MOUSE

Accession

Primary (citable) accession number: Q3TBT3
Secondary accession number(s): A7YGY9 , Q3TAV5, Q3TYP5, Q3TZY8, Q3UJW3, Q8C227, Q8C5Q3, Q8K393, Q9CZY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program