Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)

 STING_HUMAN             Reviewed;         379 AA.
Q86WV6; A8K3P6; B6EB35; D6RBX0; D6RE01; D6RID9;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Stimulator of interferon genes protein {ECO:0000303|PubMed:18724357};
Short=hSTING {ECO:0000303|PubMed:18724357, ECO:0000303|PubMed:26669264};
AltName: Full=Endoplasmic reticulum interferon stimulator;
Short=ERIS;
AltName: Full=Mediator of IRF3 activation {ECO:0000303|PubMed:18818105, ECO:0000303|PubMed:19285439};
Short=hMITA {ECO:0000303|PubMed:18818105, ECO:0000303|PubMed:19285439};
AltName: Full=Transmembrane protein 173;
Name=TMEM173;
Synonyms=ERIS, MITA {ECO:0000303|PubMed:18818105,
ECO:0000303|PubMed:19285439}, STING {ECO:0000303|PubMed:18724357,
ECO:0000303|PubMed:26669264};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INTERACTION WITH MAVS, PHOSPHORYLATION AT SER-358, AND
MUTAGENESIS OF 324-SER--SER-326 AND SER-358.
PubMed=18818105; DOI=10.1016/j.immuni.2008.09.003;
Zhong B., Yang Y., Li S., Wang Y.-Y., Li Y., Diao F., Lei C., He X.,
Zhang L., Tien P., Shu H.-B.;
"The adaptor protein MITA links virus-sensing receptors to IRF3
transcription factor activation.";
Immunity 29:538-550(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-232.
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
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.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
WITH DDX58 AND SSR2.
PubMed=18724357; DOI=10.1038/nature07317;
Ishikawa H., Barber G.N.;
"STING is an endoplasmic reticulum adaptor that facilitates innate
immune signalling.";
Nature 455:674-678(2008).
[6]
UBIQUITINATION AT LYS-150, INTERACTION WITH RNF5, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-150.
PubMed=19285439; DOI=10.1016/j.immuni.2009.01.008;
Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y.,
Zhang X.L., Shu H.B.;
"The ubiquitin ligase RNF5 regulates antiviral responses by mediating
degradation of the adaptor protein MITA.";
Immunity 30:397-407(2009).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19776740; DOI=10.1038/nature08476;
Ishikawa H., Ma Z., Barber G.N.;
"STING regulates intracellular DNA-mediated, type I interferon-
dependent innate immunity.";
Nature 461:788-792(2009).
[8]
INTERACTION WITH IFIT1; IFIT2; MAVS AND TBK1.
PubMed=19416887; DOI=10.1073/pnas.0900818106;
Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y.,
Yang F., Shu H.B.;
"ISG56 is a negative-feedback regulator of virus-triggered signaling
and cellular antiviral response.";
Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, HOMODIMERIZATION, PHOSPHORYLATION,
UBIQUITINATION, AND MUTAGENESIS OF 76-ARG--ARG-78 AND
178-ARG--ARG-180.
PubMed=19433799; DOI=10.1073/pnas.0900850106;
Sun W., Li Y., Chen L., Chen H., You F., Zhou X., Zhou Y., Zhai Z.,
Chen D., Jiang Z.;
"ERIS, an endoplasmic reticulum IFN stimulator, activates innate
immune signaling through dimerization.";
Proc. Natl. Acad. Sci. U.S.A. 106:8653-8658(2009).
[10]
FUNCTION, HOMODIMERIZATION, UBIQUITINATION AT LYS-150, AND MUTAGENESIS
OF LYS-20; LYS-137 AND LYS-150.
PubMed=21074459; DOI=10.1016/j.immuni.2010.10.013;
Tsuchida T., Zou J., Saitoh T., Kumar H., Abe T., Matsuura Y.,
Kawai T., Akira S.;
"The ubiquitin ligase TRIM56 regulates innate immune responses to
intracellular double-stranded DNA.";
Immunity 33:765-776(2010).
[11]
FUNCTION, AND C-DI-GMP-BINDING.
PubMed=21947006; DOI=10.1038/nature10429;
Burdette D.L., Monroe K.M., Sotelo-Troha K., Iwig J.S., Eckert B.,
Hyodo M., Hayakawa Y., Vance R.E.;
"STING is a direct innate immune sensor of cyclic di-GMP.";
Nature 478:515-518(2011).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23027953; DOI=10.1073/pnas.1211302109;
Orzalli M.H., DeLuca N.A., Knipe D.M.;
"Nuclear IFI16 induction of IRF-3 signaling during herpesviral
infection and degradation of IFI16 by the viral ICP0 protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012).
[13]
FUNCTION.
PubMed=23707065; DOI=10.1016/j.celrep.2013.05.009;
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.;
"The innate immune DNA sensor cGAS produces a noncanonical cyclic
dinucleotide that activates human STING.";
Cell Rep. 3:1355-1361(2013).
[14]
FUNCTION.
PubMed=23722158; DOI=10.1038/nature12306;
Ablasser A., Goldeck M., Cavlar T., Deimling T., Witte G., Rohl I.,
Hopfner K.P., Ludwig J., Hornung V.;
"cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger
that activates STING.";
Nature 498:380-384(2013).
[15]
FUNCTION.
PubMed=23258412; DOI=10.1126/science.1229963;
Wu J., Sun L., Chen X., Du F., Shi H., Chen C., Chen Z.J.;
"Cyclic GMP-AMP is an endogenous second messenger in innate immune
signaling by cytosolic DNA.";
Science 339:826-830(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
TISSUE SPECIFICITY, AND VARIANTS SAVI LEU-147; SER-154 AND MET-155.
PubMed=25029335; DOI=10.1056/NEJMoa1312625;
Liu Y., Jesus A.A., Marrero B., Yang D., Ramsey S.E.,
Montealegre Sanchez G.A., Tenbrock K., Wittkowski H., Jones O.Y.,
Kuehn H.S., Lee C.C., DiMattia M.A., Cowen E.W., Gonzalez B.,
Palmer I., DiGiovanna J.J., Biancotto A., Kim H., Tsai W.L.,
Trier A.M., Huang Y., Stone D.L., Hill S., Kim H.J., St Hilaire C.,
Gurprasad S., Plass N., Chapelle D., Horkayne-Szakaly I., Foell D.,
Barysenka A., Candotti F., Holland S.M., Hughes J.D., Mehmet H.,
Issekutz A.C., Raffeld M., McElwee J., Fontana J.R., Minniti C.P.,
Moir S., Kastner D.L., Gadina M., Steven A.C., Wingfield P.T.,
Brooks S.R., Rosenzweig S.D., Fleisher T.A., Deng Z., Boehm M.,
Paller A.S., Goldbach-Mansky R.;
"Activated STING in a vascular and pulmonary syndrome.";
N. Engl. J. Med. 371:507-518(2014).
[18]
UBIQUITINATION AT LYS-150, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-150.
PubMed=25254379; DOI=10.1371/journal.ppat.1004358;
Qin Y., Zhou M.T., Hu M.M., Hu Y.H., Zhang J., Guo L., Zhong B.,
Shu H.B.;
"RNF26 temporally regulates virus-triggered type I interferon
induction by two distinct mechanisms.";
PLoS Pathog. 10:E1004358-E1004358(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
FUNCTION, MUTAGENESIS OF SER-162, AND MISCELLANEOUS.
PubMed=26669264; DOI=10.1038/srep18035;
Zhang H., Han M.J., Tao J., Ye Z.Y., Du X.X., Deng M.J., Zhang X.Y.,
Li L.F., Jiang Z.F., Su X.D.;
"Rat and human STINGs profile similarly towards anticancer/antiviral
compounds.";
Sci. Rep. 5:18035-18035(2015).
[21]
CHARACTERIZATION OF VARIANT ARG-232, AND FUNCTION.
PubMed=26300263; DOI=10.1016/j.molcel.2015.07.022;
Kranzusch P.J., Wilson S.C., Lee A.S., Berger J.M., Doudna J.A.,
Vance R.E.;
"Ancient origin of cGAS-STING reveals mechanism of universal 2',3'
cGAMP signaling.";
Mol. Cell 59:891-903(2015).
[22]
FUNCTION.
PubMed=26229117; DOI=10.1126/science.aab3632;
Bridgeman A., Maelfait J., Davenne T., Partridge T., Peng Y.,
Mayer A., Dong T., Kaever V., Borrow P., Rehwinkel J.;
"Viruses transfer the antiviral second messenger cGAMP between
cells.";
Science 349:1228-1232(2015).
[23]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH PAPILLOMAVIRUS
PROTEIN E7 AND ADENOVIRUS EARLY E1A PROTEIN (MICROBIAL INFECTION).
PubMed=26405230; DOI=10.1126/science.aab3291;
Lau L., Gray E.E., Brunette R.L., Stetson D.B.;
"DNA tumor virus oncogenes antagonize the cGAS-STING DNA-sensing
pathway.";
Science 350:568-571(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 139-379, SUBUNIT, AND
C-DI-GMP-BINDING.
PubMed=22579474; DOI=10.1016/j.immuni.2012.03.019;
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.;
"Structural analysis of the STING adaptor protein reveals a
hydrophobic dimer interface and mode of cyclic di-GMP binding.";
Immunity 36:1073-1086(2012).
[25]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 139-379, SUBUNIT, AND
C-DI-GMP-BINDING.
PubMed=22705373; DOI=10.1016/j.molcel.2012.05.029;
Yin Q., Tian Y., Kabaleeswaran V., Jiang X., Tu D., Eck M.J.,
Chen Z.J., Wu H.;
"Cyclic di-GMP sensing via the innate immune signaling protein
STING.";
Mol. Cell 46:735-745(2012).
[26]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 155-341, SUBUNIT,
C-DI-GMP-BINDING, AND MUTAGENESIS OF SER-162; GLY-166; TYR-240;
ASN-242; GLU-260; THR-263; PRO-264 AND THR-267.
PubMed=22728658; DOI=10.1038/nsmb.2331;
Shu C., Yi G., Watts T., Kao C.C., Li P.;
"Structure of STING bound to cyclic di-GMP reveals the mechanism of
cyclic dinucleotide recognition by the immune system.";
Nat. Struct. Mol. Biol. 19:722-724(2012).
[27]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 149-379, SUBUNIT, AND
C-DI-GMP-BINDING.
PubMed=22728660; DOI=10.1038/nsmb.2332;
Shang G., Zhu D., Li N., Zhang J., Zhu C., Lu D., Liu C., Yu Q.,
Zhao Y., Xu S., Gu L.;
"Crystal structures of STING protein reveal basis for recognition of
cyclic di-GMP.";
Nat. Struct. Mol. Biol. 19:725-727(2012).
[28]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 141-379, SUBUNIT, AND
C-DI-GMP-BINDING.
PubMed=22728659; DOI=10.1038/nsmb.2333;
Huang Y.H., Liu X.Y., Du X.X., Jiang Z.F., Su X.D.;
"The structural basis for the sensing and binding of cyclic di-GMP by
STING.";
Nat. Struct. Mol. Biol. 19:728-730(2012).
-!- 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. 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).
{ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105,
ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740,
ECO:0000269|PubMed:21074459, ECO:0000269|PubMed:21947006,
ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:23258412,
ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722158,
ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263,
ECO:0000269|PubMed:26669264}.
-!- FUNCTION: (Microbial infection) Antiviral activity is antagonized
by oncoproteins, such as papillomavirus (HPV) protein E7 and
adenovirus early E1A protein (PubMed:26405230). Such oncoproteins
prevent the ability to sense cytosolic DNA (PubMed:26405230).
{ECO:0000269|PubMed:26405230}.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:18724357,
ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19285439,
ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:22579474,
ECO:0000269|PubMed:22705373, ECO:0000269|PubMed:22728658,
ECO:0000269|PubMed:22728659, ECO:0000269|PubMed:22728660}.
-!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
(HPV) protein E7 (PubMed:26405230). Interacts with adenovirus
early E1A protein (PubMed:26405230).
{ECO:0000269|PubMed:26405230}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-2800345, EBI-2800345;
P03255:- (xeno); NbExp=2; IntAct=EBI-2800345, EBI-2603114;
P27958:- (xeno); NbExp=5; IntAct=EBI-2800345, EBI-8763498;
Q99IB8:- (xeno); NbExp=5; IntAct=EBI-2800345, EBI-6928570;
Q96A33:CCDC47; NbExp=2; IntAct=EBI-2800345, EBI-720151;
P39656:DDOST; NbExp=2; IntAct=EBI-2800345, EBI-358866;
O95786-1:DDX58; NbExp=2; IntAct=EBI-2800345, EBI-15577823;
Q16666:IFI16; NbExp=2; IntAct=EBI-2800345, EBI-2867186;
P09914:IFIT1; NbExp=3; IntAct=EBI-2800345, EBI-745117;
P09913:IFIT2; NbExp=3; IntAct=EBI-2800345, EBI-3507167;
P51617:IRAK1; NbExp=2; IntAct=EBI-2800345, EBI-358664;
O94822:LTN1; NbExp=2; IntAct=EBI-2800345, EBI-1044684;
Q7Z434:MAVS; NbExp=7; IntAct=EBI-2800345, EBI-995373;
Q7Z434-1:MAVS; NbExp=7; IntAct=EBI-2800345, EBI-15577799;
Q96N66:MBOAT7; NbExp=2; IntAct=EBI-2800345, EBI-6116499;
O95470:SGPL1; NbExp=2; IntAct=EBI-2800345, EBI-1046170;
P43308:SSR2; NbExp=4; IntAct=EBI-2800345, EBI-2822012;
P42226:STAT6; NbExp=12; IntAct=EBI-2800345, EBI-1186478;
P46977:STT3A; NbExp=2; IntAct=EBI-2800345, EBI-719212;
O15260:SURF4; NbExp=2; IntAct=EBI-2800345, EBI-1044848;
Q9UHD2:TBK1; NbExp=8; IntAct=EBI-2800345, EBI-356402;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:19285439,
ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740,
ECO:0000269|PubMed:25254379}; Multi-pass membrane protein
{ECO:0000255}. Mitochondrion outer membrane
{ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:19285439,
ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740}; Multi-
pass membrane protein {ECO:0000255}. Cell membrane
{ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:19433799}. Cytoplasm
{ECO:0000269|PubMed:23027953}. Note=In response to double-stranded
DNA stimulation, relocalizes to perinuclear region, where the
kinase TBK1 is recruited.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in skin
endothelial cells, alveolar type 2 pneumocytes, bronchial
epithelium and alveolar macrophages. {ECO:0000269|PubMed:18724357,
ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:25029335}.
-!- 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
(PubMed:22579474, PubMed:22705373, PubMed:22728658,
PubMed:22728660 and PubMed:22728659).
-!- PTM: Phosphorylated on tyrosine residues upon MHC-II aggregation
(By similarity). Phosphorylated on Ser-358 by TBK1, leading to
activation and production of IFN-beta. {ECO:0000250,
ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799}.
-!- PTM: Ubiquitinated (PubMed:19285439, PubMed:19433799,
PubMed:21074459, PubMed:25254379). '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 (PubMed:21074459). 'Lys-48'-linked polyubiquitination
at Lys-150 occurring after viral infection is mediated by RNF5 and
leads to proteasomal degradation (PubMed:19285439). 'Lys-11'-
linked polyubiquitination at Lys-150 by RNF26 leads to stabilize
TMEM173/STING: it protects TMEM173/STING from RNF5-mediated 'Lys-
48'-linked polyubiquitination (PubMed:25254379).
{ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:19433799,
ECO:0000269|PubMed:21074459, ECO:0000269|PubMed:25254379}.
-!- DISEASE: STING-associated vasculopathy, infantile-onset (SAVI)
[MIM:615934]: An 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.
{ECO:0000269|PubMed:25029335}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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).
{ECO:0000269|PubMed:26669264}.
-!- SIMILARITY: Belongs to the TMEM173 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; FJ222241; ACI46648.1; -; mRNA.
EMBL; AK290661; BAF83350.1; -; mRNA.
EMBL; AC138517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC047779; AAH47779.1; -; mRNA.
CCDS; CCDS4215.1; -.
RefSeq; NP_938023.1; NM_198282.3.
UniGene; Hs.379754; -.
PDB; 4EF4; X-ray; 2.15 A; A/B=139-379.
PDB; 4EF5; X-ray; 2.45 A; A=139-379.
PDB; 4EMT; X-ray; 1.50 A; A/B=155-341.
PDB; 4EMU; X-ray; 1.90 A; A/B=155-341.
PDB; 4F5D; X-ray; 3.00 A; A/B=141-379.
PDB; 4F5E; X-ray; 2.60 A; A=141-379.
PDB; 4F5W; X-ray; 2.20 A; A=149-379.
PDB; 4F5Y; X-ray; 2.40 A; A/B=149-379.
PDB; 4F9E; X-ray; 2.75 A; A=139-379.
PDB; 4F9G; X-ray; 2.95 A; A/C=139-379.
PDB; 4KSY; X-ray; 1.88 A; A=138-379.
PDB; 4LOH; X-ray; 2.25 A; A/B=155-341.
PDB; 4LOI; X-ray; 1.89 A; A/B=155-341.
PDB; 4QXO; X-ray; 1.88 A; A=155-341.
PDB; 4QXP; X-ray; 2.51 A; A/B=155-341.
PDB; 4QXQ; X-ray; 2.42 A; A/B=155-341.
PDB; 4QXR; X-ray; 2.37 A; A/B=155-341.
PDB; 5BQX; X-ray; 2.00 A; A=138-379.
PDB; 5JEJ; X-ray; 2.00 A; C/D/E=342-377.
PDBsum; 4EF4; -.
PDBsum; 4EF5; -.
PDBsum; 4EMT; -.
PDBsum; 4EMU; -.
PDBsum; 4F5D; -.
PDBsum; 4F5E; -.
PDBsum; 4F5W; -.
PDBsum; 4F5Y; -.
PDBsum; 4F9E; -.
PDBsum; 4F9G; -.
PDBsum; 4KSY; -.
PDBsum; 4LOH; -.
PDBsum; 4LOI; -.
PDBsum; 4QXO; -.
PDBsum; 4QXP; -.
PDBsum; 4QXQ; -.
PDBsum; 4QXR; -.
PDBsum; 5BQX; -.
PDBsum; 5JEJ; -.
ProteinModelPortal; Q86WV6; -.
SMR; Q86WV6; -.
BioGrid; 130988; 45.
DIP; DIP-48847N; -.
IntAct; Q86WV6; 37.
STRING; 9606.ENSP00000331288; -.
GuidetoPHARMACOLOGY; 2902; -.
iPTMnet; Q86WV6; -.
PhosphoSitePlus; Q86WV6; -.
SwissPalm; Q86WV6; -.
BioMuta; TMEM173; -.
DMDM; 74727720; -.
EPD; Q86WV6; -.
MaxQB; Q86WV6; -.
PaxDb; Q86WV6; -.
PeptideAtlas; Q86WV6; -.
PRIDE; Q86WV6; -.
DNASU; 340061; -.
Ensembl; ENST00000330794; ENSP00000331288; ENSG00000184584.
GeneID; 340061; -.
KEGG; hsa:340061; -.
UCSC; uc003lep.4; human.
CTD; 340061; -.
DisGeNET; 340061; -.
EuPathDB; HostDB:ENSG00000184584.12; -.
GeneCards; TMEM173; -.
HGNC; HGNC:27962; TMEM173.
HPA; HPA038116; -.
HPA; HPA038534; -.
MalaCards; TMEM173; -.
MIM; 612374; gene.
MIM; 615934; phenotype.
neXtProt; NX_Q86WV6; -.
OpenTargets; ENSG00000184584; -.
PharmGKB; PA162405934; -.
eggNOG; ENOG410IH2R; Eukaryota.
eggNOG; ENOG4111M85; LUCA.
GeneTree; ENSGT00390000008582; -.
HOGENOM; HOG000076316; -.
HOVERGEN; HBG094065; -.
InParanoid; Q86WV6; -.
KO; K12654; -.
OMA; LIVYQEP; -.
OrthoDB; EOG091G08B2; -.
PhylomeDB; Q86WV6; -.
TreeFam; TF324444; -.
Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-3249367; STAT6-mediated induction of chemokines.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; TMEM173; human.
GenomeRNAi; 340061; -.
PRO; PR:Q86WV6; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000184584; -.
CleanEx; HS_TMEM173; -.
ExpressionAtlas; Q86WV6; baseline and differential.
Genevisible; Q86WV6; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0035438; F:cyclic-di-GMP binding; IDA:UniProtKB.
GO; GO:0061507; F:cyclic-GMP-AMP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0002218; P:activation of innate immune response; IMP:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:BHF-UCL.
GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0032608; P:interferon-beta production; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IDA:BHF-UCL.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
CDD; cd12146; STING_C; 1.
InterPro; IPR029158; STING.
InterPro; IPR033952; STING_C.
Pfam; PF15009; TMEM173; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Cell membrane; Complete proteome; Cytoplasm;
Disease mutation; Endoplasmic reticulum; Host-virus interaction;
Immunity; Innate immunity; Isopeptide bond; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 379 Stimulator of interferon genes protein.
/FTId=PRO_0000271116.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 42 46 Extracellular. {ECO:0000255}.
TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 68 86 Cytoplasmic. {ECO:0000255}.
TRANSMEM 87 106 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 107 115 Extracellular. {ECO:0000255}.
TRANSMEM 116 136 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 137 379 Cytoplasmic. {ECO:0000255}.
REGION 153 340 c-di-GMP-binding domain (CBD).
REGION 162 167 c-di-GMP binding.
REGION 238 241 c-di-GMP binding.
REGION 340 379 C-terminal tail (CTT).
BINDING 263 263 c-di-GMP.
MOD_RES 358 358 Phosphoserine; by TBK1.
{ECO:0000269|PubMed:18818105}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19285439,
ECO:0000269|PubMed:21074459}.
VARIANT 71 71 R -> H (in dbSNP:rs11554776).
/FTId=VAR_029863.
VARIANT 147 147 V -> L (in SAVI; dbSNP:rs587777611).
{ECO:0000269|PubMed:25029335}.
/FTId=VAR_071878.
VARIANT 154 154 N -> S (in SAVI; dbSNP:rs587777609).
{ECO:0000269|PubMed:25029335}.
/FTId=VAR_071879.
VARIANT 155 155 V -> M (in SAVI; dbSNP:rs587777610).
{ECO:0000269|PubMed:25029335}.
/FTId=VAR_071880.
VARIANT 232 232 H -> R (activated by both 2'-3' linked
cGAMP and 3'-3' linked cGAMP;
dbSNP:rs1131769).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:26300263}.
/FTId=VAR_029864.
VARIANT 293 293 R -> Q (in dbSNP:rs7380824).
/FTId=VAR_029865.
MUTAGEN 20 20 K->R: Does not affect amount of
ubiquitination.
{ECO:0000269|PubMed:21074459}.
MUTAGEN 76 78 RYR->AYA: Abolishes the endoplasmic
reticulum location.
{ECO:0000269|PubMed:19433799}.
MUTAGEN 137 137 K->R: Does not affect amount of
ubiquitination.
{ECO:0000269|PubMed:21074459}.
MUTAGEN 150 150 K->R: Abolishes ubiquitination,
homodimerization and subsequent
production of IFN-beta.
{ECO:0000269|PubMed:19285439,
ECO:0000269|PubMed:21074459,
ECO:0000269|PubMed:25254379}.
MUTAGEN 162 162 S->A: Slight decrease in c-di-GMP-
binding. Strongly increases response to
the synthetic compound 5,6-
dimethylxanthenone 4-acetic acid (DMXAA).
{ECO:0000269|PubMed:22728658,
ECO:0000269|PubMed:26669264}.
MUTAGEN 166 166 G->S: Slight decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 178 180 RIR->AIA: Abolishes the endoplasmic
reticulum location.
{ECO:0000269|PubMed:19433799}.
MUTAGEN 240 240 Y->S: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 242 242 N->A: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 260 260 E->A: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 263 263 T->A: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 264 264 P->A: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 267 267 T->A: Strong decrease in c-di-GMP-
binding. {ECO:0000269|PubMed:22728658}.
MUTAGEN 324 326 SLS->ALA: Induces a decrease in
phosphorylation by TBK1.
{ECO:0000269|PubMed:18818105}.
MUTAGEN 358 358 S->A: Induces a decrease in
phosphorylation by TBK1 and ability to
activate IRF-E.
{ECO:0000269|PubMed:18818105}.
CONFLICT 262 262 A -> T (in Ref. 2; BAF83350).
{ECO:0000305}.
CONFLICT 363 363 L -> F (in Ref. 2; BAF83350).
{ECO:0000305}.
HELIX 156 166 {ECO:0000244|PDB:4EMT}.
HELIX 168 185 {ECO:0000244|PDB:4EMT}.
TURN 186 189 {ECO:0000244|PDB:4EMT}.
STRAND 196 203 {ECO:0000244|PDB:4EMT}.
HELIX 212 215 {ECO:0000244|PDB:4EMT}.
STRAND 219 225 {ECO:0000244|PDB:4EMT}.
STRAND 228 230 {ECO:0000244|PDB:4QXO}.
STRAND 233 235 {ECO:0000244|PDB:4F5E}.
STRAND 237 240 {ECO:0000244|PDB:4QXO}.
STRAND 242 249 {ECO:0000244|PDB:4EMT}.
STRAND 252 261 {ECO:0000244|PDB:4EMT}.
HELIX 264 272 {ECO:0000244|PDB:4EMT}.
HELIX 275 277 {ECO:0000244|PDB:4EMT}.
HELIX 281 301 {ECO:0000244|PDB:4EMT}.
HELIX 303 306 {ECO:0000244|PDB:4EMT}.
STRAND 309 314 {ECO:0000244|PDB:4EMT}.
STRAND 318 320 {ECO:0000244|PDB:4QXP}.
HELIX 325 333 {ECO:0000244|PDB:4EMT}.
TURN 334 336 {ECO:0000244|PDB:4EMT}.
HELIX 372 374 {ECO:0000244|PDB:5JEJ}.
SEQUENCE 379 AA; 42193 MW; CB54D6A4D4D8E7C0 CRC64;
MPHSSLHPSI PCPRGHGAQK AALVLLSACL VTLWGLGEPP EHTLRYLVLH LASLQLGLLL
NGVCSLAEEL RHIHSRYRGS YWRTVRACLG CPLRRGALLL LSIYFYYSLP NAVGPPFTWM
LALLGLSQAL NILLGLKGLA PAEISAVCEK GNFNVAHGLA WSYYIGYLRL ILPELQARIR
TYNQHYNNLL RGAVSQRLYI LLPLDCGVPD NLSMADPNIR FLDKLPQQTG DHAGIKDRVY
SNSIYELLEN GQRAGTCVLE YATPLQTLFA MSQYSQAGFS REDRLEQAKL FCRTLEDILA
DAPESQNNCR LIAYQEPADD SSFSLSQEVL RHLRQEEKEE VTVGSLKTSA VPSTSTMSQE
PELLISGMEK PLPLRTDFS


Related products :

Catalog number Product name Quantity
EIAAB42701 Endoplasmic reticulum interferon stimulator,ERIS,ERIS,hMITA,Homo sapiens,hSTING,Human,Mediator of IRF3 activation,MITA,Stimulator of interferon genes protein,STING,TMEM173,Transmembrane protein 173
EIAAB42699 Endoplasmic reticulum interferon stimulator,ERIS,Eris Mita,Mediator of IRF3 activation,MMITA,Mouse,Mpys,mSTING,Mus musculus,Stimulator of interferon genes protein,Sting,Tmem173,Transmembrane protein 1
EIAAB42698 Pig,poSTING,Stimulator of interferon genes protein,STING,Sus scrofa,TMEM173,Transmembrane protein 173
EIAAB42700 Bos taurus,Bovine,Stimulator of interferon genes protein,STING,STING,TMEM173,Transmembrane protein 173
STING_PIG Pig ELISA Kit FOR Stimulator of interferon genes protein 96T
E0281m Human ELISA Kit FOR Stimulator of interferon genes protein 96T
LYPA2_MOUSE Human ELISA Kit FOR Stimulator of interferon genes protein 96T
BHMT2_HUMAN Human ELISA Kit FOR Stimulator of interferon genes protein 96T
STING_CHICK Chicken ELISA Kit FOR Stimulator of interferon genes protein 96T
EIAAB42702 Chicken,Gallus gallus,Stimulator of interferon genes protein,STING,STING,TMEM173,Transmembrane protein 173
EIAAB07436 CDGSH iron-sulfur domain-containing protein 2,CDGSH2,CISD2,Endoplasmic reticulum intermembrane small protein,ERIS,Homo sapiens,Human,Miner1,MitoNEET-related 1 protein,NAF-1,Nutrient-deprivation autoph
EIAAB36181 Bos taurus,Bovine,Radical S-adenosyl methionine domain-containing protein 2,RSAD2,Viperin,Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
EIAAB36183 Mouse,Mus musculus,Radical S-adenosyl methionine domain-containing protein 2,Rsad2,Vig1,Viperin,Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
EIAAB44606 Endoplasmic reticulum resident protein 18,Endoplasmic reticulum resident protein 19,ER protein 18,ER protein 19,ERp18,ERp19,Homo sapiens,hTLP19,Human,Thioredoxin domain-containing protein 12,Thioredox
U1497b CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prote 96T
E1497b ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prot 96T
U1497r CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
E1497r ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
E1497m ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
E1497h ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
U1497m CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
U1497h CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
STING-101AP Stimulator of Interferon Gene protien Polyclonal anbtibody Host: Rabbit Affinity purifed 200ul
E1497b ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER 96T
E1497h ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur