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Protein

Stimulator of interferon genes protein

Gene

TMEM173

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Exhibits 2',3' phosphodiester linkage-specific ligand recognition. Can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263).13 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei263c-di-GMP1

GO - Molecular functioni

  • cyclic-di-GMP binding Source: UniProtKB
  • cyclic-GMP-AMP binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

  • activation of innate immune response Source: BHF-UCL
  • apoptotic process Source: UniProtKB-KW
  • cellular response to exogenous dsRNA Source: BHF-UCL
  • cellular response to interferon-beta Source: Ensembl
  • cellular response to organic cyclic compound Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB
  • interferon-beta production Source: UniProtKB
  • positive regulation of defense response to virus by host Source: BHF-UCL
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of protein import into nucleus, translocation Source: BHF-UCL
  • positive regulation of transcription factor import into nucleus Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of type I interferon production Source: UniProtKB
  • 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

BioCyciZFISH:G66-32478-MONOMER.
ReactomeiR-HSA-1606341. IRF3 mediated activation of type 1 IFN.
R-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3249367. STAT6-mediated induction of chemokines.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Stimulator of interferon genes protein1 Publication
Short name:
hSTING2 Publications
Alternative name(s):
Endoplasmic reticulum interferon stimulator
Short name:
ERIS
Mediator of IRF3 activation2 Publications
Short name:
hMITA2 Publications
Transmembrane protein 173
Gene namesi
Name:TMEM173
Synonyms:ERIS, MITA2 Publications, STING2 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:27962. TMEM173.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20CytoplasmicSequence analysisAdd BLAST20
Transmembranei21 – 41Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini42 – 46ExtracellularSequence analysis5
Transmembranei47 – 67Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini68 – 86CytoplasmicSequence analysisAdd BLAST19
Transmembranei87 – 106Helical; Name=3Sequence analysisAdd BLAST20
Topological domaini107 – 115ExtracellularSequence analysis9
Transmembranei116 – 136Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini137 – 379CytoplasmicSequence analysisAdd BLAST243

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

STING-associated vasculopathy, infantile-onset (SAVI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autoinflammatory disease characterized by early-onset systemic inflammation and cutaneous vasculopathy, resulting in severe skin lesions. Violaceous, scaling lesions of fingers, toes, nose, cheeks and ears progress to acral necrosis in most of the patients. Some patients have severe interstitial lung disease.
See also OMIM:615934
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071878147V → L in SAVI. 1 PublicationCorresponds to variant rs587777611dbSNPEnsembl.1
Natural variantiVAR_071879154N → S in SAVI. 1 PublicationCorresponds to variant rs587777609dbSNPEnsembl.1
Natural variantiVAR_071880155V → M in SAVI. 1 PublicationCorresponds to variant rs587777610dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20K → R: Does not affect amount of ubiquitination. 1 Publication1
Mutagenesisi76 – 78RYR → AYA: Abolishes the endoplasmic reticulum location. 1 Publication3
Mutagenesisi137K → R: Does not affect amount of ubiquitination. 1 Publication1
Mutagenesisi150K → R: Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta. 2 Publications1
Mutagenesisi162S → A: Slight decrease in c-di-GMP-binding. Strongly increases response to the synthetic compound 5,6-dimethylxanthenone 4-acetic acid (DMXAA). 2 Publications1
Mutagenesisi166G → S: Slight decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi178 – 180RIR → AIA: Abolishes the endoplasmic reticulum location. 1 Publication3
Mutagenesisi240Y → S: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi242N → A: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi260E → A: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi263T → A: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi264P → A: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi267T → A: Strong decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi324 – 326SLS → ALA: Induces a decrease in phosphorylation by TBK1. 1 Publication3
Mutagenesisi358S → A: Induces a decrease in phosphorylation by TBK1 and ability to activate IRF-E. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi340061.
MalaCardsiTMEM173.
MIMi615934. phenotype.
OpenTargetsiENSG00000184584.
PharmGKBiPA162405934.

Chemistry databases

GuidetoPHARMACOLOGYi2902.

Polymorphism and mutation databases

BioMutaiTMEM173.
DMDMi74727720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002711161 – 379Stimulator of interferon genes proteinAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei358Phosphoserine; by TBK11 Publication1

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.By similarity2 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

EPDiQ86WV6.
MaxQBiQ86WV6.
PaxDbiQ86WV6.
PeptideAtlasiQ86WV6.
PRIDEiQ86WV6.

PTM databases

iPTMnetiQ86WV6.
PhosphoSitePlusiQ86WV6.
SwissPalmiQ86WV6.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed in skin endothelial cells, alveolar type 2 pneumocytes, bronchial epithelium and alveolar macrophages.3 Publications

Gene expression databases

BgeeiENSG00000184584.
CleanExiHS_TMEM173.
ExpressionAtlasiQ86WV6. baseline and differential.
GenevisibleiQ86WV6. HS.

Organism-specific databases

HPAiHPA038116.
HPA038534.

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.By similarity9 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

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi130988. 33 interactors.
DIPiDIP-48847N.
IntActiQ86WV6. 29 interactors.
STRINGi9606.ENSP00000331288.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi156 – 166Combined sources11
Helixi168 – 185Combined sources18
Turni186 – 189Combined sources4
Beta strandi196 – 203Combined sources8
Helixi212 – 215Combined sources4
Beta strandi219 – 225Combined sources7
Beta strandi228 – 230Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi237 – 240Combined sources4
Beta strandi242 – 249Combined sources8
Beta strandi252 – 261Combined sources10
Helixi264 – 272Combined sources9
Helixi275 – 277Combined sources3
Helixi281 – 301Combined sources21
Helixi303 – 306Combined sources4
Beta strandi309 – 314Combined sources6
Beta strandi318 – 320Combined sources3
Helixi325 – 333Combined sources9
Turni334 – 336Combined sources3
Helixi372 – 374Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QXOX-ray1.88A155-341[»]
4QXPX-ray2.51A/B155-341[»]
4QXQX-ray2.42A/B155-341[»]
4QXRX-ray2.37A/B155-341[»]
5BQXX-ray2.00A138-379[»]
5JEJX-ray2.00C/D/E342-377[»]
ProteinModelPortaliQ86WV6.
SMRiQ86WV6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni153 – 340c-di-GMP-binding domain (CBD)Add BLAST188
Regioni162 – 167c-di-GMP binding6
Regioni238 – 241c-di-GMP binding4
Regioni340 – 379C-terminal tail (CTT)Add BLAST40

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 (PubMed:22579474, PubMed:22705373, PubMed:22728658, PubMed:22728660 and PubMed:22728659).

Sequence similaritiesi

Belongs to the TMEM173 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IH2R. Eukaryota.
ENOG4111M85. LUCA.
GeneTreeiENSGT00390000008582.
HOGENOMiHOG000076316.
HOVERGENiHBG094065.
InParanoidiQ86WV6.
KOiK12654.
OMAiTWMLALL.
OrthoDBiEOG091G08B2.
PhylomeDBiQ86WV6.
TreeFamiTF324444.

Family and domain databases

CDDicd12146. STING_C. 1 hit.
InterProiIPR029158. STING.
IPR033952. STING_C.
[Graphical view]
PfamiPF15009. TMEM173. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86WV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSSLHPSI PCPRGHGAQK AALVLLSACL VTLWGLGEPP EHTLRYLVLH
60 70 80 90 100
LASLQLGLLL NGVCSLAEEL RHIHSRYRGS YWRTVRACLG CPLRRGALLL
110 120 130 140 150
LSIYFYYSLP NAVGPPFTWM LALLGLSQAL NILLGLKGLA PAEISAVCEK
160 170 180 190 200
GNFNVAHGLA WSYYIGYLRL ILPELQARIR TYNQHYNNLL RGAVSQRLYI
210 220 230 240 250
LLPLDCGVPD NLSMADPNIR FLDKLPQQTG DHAGIKDRVY SNSIYELLEN
260 270 280 290 300
GQRAGTCVLE YATPLQTLFA MSQYSQAGFS REDRLEQAKL FCRTLEDILA
310 320 330 340 350
DAPESQNNCR LIAYQEPADD SSFSLSQEVL RHLRQEEKEE VTVGSLKTSA
360 370
VPSTSTMSQE PELLISGMEK PLPLRTDFS
Length:379
Mass (Da):42,193
Last modified:June 1, 2003 - v1
Checksum:iCB54D6A4D4D8E7C0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262A → T in BAF83350 (PubMed:14702039).Curated1
Sequence conflicti363L → F in BAF83350 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02986371R → H.Corresponds to variant rs11554776dbSNPEnsembl.1
Natural variantiVAR_071878147V → L in SAVI. 1 PublicationCorresponds to variant rs587777611dbSNPEnsembl.1
Natural variantiVAR_071879154N → S in SAVI. 1 PublicationCorresponds to variant rs587777609dbSNPEnsembl.1
Natural variantiVAR_071880155V → M in SAVI. 1 PublicationCorresponds to variant rs587777610dbSNPEnsembl.1
Natural variantiVAR_029864232H → R Activated by both 2'-3' linked cGAMP and 3'-3' linked cGAMP. 2 PublicationsCorresponds to variant rs1131769dbSNPEnsembl.1
Natural variantiVAR_029865293R → Q.Corresponds to variant rs7380824dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_198282.3.
UniGeneiHs.379754.

Genome annotation databases

EnsembliENST00000330794; ENSP00000331288; ENSG00000184584.
GeneIDi340061.
KEGGihsa:340061.
UCSCiuc003lep.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_198282.3.
UniGeneiHs.379754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QXOX-ray1.88A155-341[»]
4QXPX-ray2.51A/B155-341[»]
4QXQX-ray2.42A/B155-341[»]
4QXRX-ray2.37A/B155-341[»]
5BQXX-ray2.00A138-379[»]
5JEJX-ray2.00C/D/E342-377[»]
ProteinModelPortaliQ86WV6.
SMRiQ86WV6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130988. 33 interactors.
DIPiDIP-48847N.
IntActiQ86WV6. 29 interactors.
STRINGi9606.ENSP00000331288.

Chemistry databases

GuidetoPHARMACOLOGYi2902.

PTM databases

iPTMnetiQ86WV6.
PhosphoSitePlusiQ86WV6.
SwissPalmiQ86WV6.

Polymorphism and mutation databases

BioMutaiTMEM173.
DMDMi74727720.

Proteomic databases

EPDiQ86WV6.
MaxQBiQ86WV6.
PaxDbiQ86WV6.
PeptideAtlasiQ86WV6.
PRIDEiQ86WV6.

Protocols and materials databases

DNASUi340061.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330794; ENSP00000331288; ENSG00000184584.
GeneIDi340061.
KEGGihsa:340061.
UCSCiuc003lep.4. human.

Organism-specific databases

CTDi340061.
DisGeNETi340061.
GeneCardsiTMEM173.
HGNCiHGNC:27962. TMEM173.
HPAiHPA038116.
HPA038534.
MalaCardsiTMEM173.
MIMi612374. gene.
615934. phenotype.
neXtProtiNX_Q86WV6.
OpenTargetsiENSG00000184584.
PharmGKBiPA162405934.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH2R. Eukaryota.
ENOG4111M85. LUCA.
GeneTreeiENSGT00390000008582.
HOGENOMiHOG000076316.
HOVERGENiHBG094065.
InParanoidiQ86WV6.
KOiK12654.
OMAiTWMLALL.
OrthoDBiEOG091G08B2.
PhylomeDBiQ86WV6.
TreeFamiTF324444.

Enzyme and pathway databases

BioCyciZFISH:G66-32478-MONOMER.
ReactomeiR-HSA-1606341. IRF3 mediated activation of type 1 IFN.
R-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3249367. STAT6-mediated induction of chemokines.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiTMEM173. human.
GenomeRNAii340061.
PROiQ86WV6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184584.
CleanExiHS_TMEM173.
ExpressionAtlasiQ86WV6. baseline and differential.
GenevisibleiQ86WV6. HS.

Family and domain databases

CDDicd12146. STING_C. 1 hit.
InterProiIPR029158. STING.
IPR033952. STING_C.
[Graphical view]
PfamiPF15009. TMEM173. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 111 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

Miscellaneous

Contrary to human and rat TMEM173/STING, mouse TMEM173/STING mediates not only responses to cyclic nucleotide signaling molecules, but is also strongly activated by antiviral and anticancer molecules, such as 5,6-dimethylxanthenone 4-acetic acid (DMXAA) and 10-carboxymethyl-9-acridanone (CMA).1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.