| UniProt ID | STING_HUMAN | |
|---|---|---|
| UniProt AC | Q86WV6 | |
| Protein Name | Stimulator of interferon genes protein {ECO:0000303|PubMed:18724357} | |
| Gene Name | TMEM173 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 379 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Mitochondrion outer membrane Multi-pass membrane protein . Cell membrane Multi-pass membrane protein . Cytoplasm, perinuclear region . Cytoplasm . In response to double-stranded DNA s |
|
| Protein Description | 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; (Microbial infection) Antiviral activity is antagonized by oncoproteins, such as papillomavirus (HPV) protein E7 and adenovirus early E1A protein] | |
| Protein Sequence | MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLLNGVCSLAEELRHIHSRYRGSYWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWMLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 20 | Ubiquitination | PRGHGAQKAALVLLS CCCCHHHHHHHHHHH | PubMed | ||
| 84 | Phosphorylation | YRGSYWRTVRACLGC HCCCHHHHHHHHHCC | 27251275 | ||
| 137 | Ubiquitination | LNILLGLKGLAPAEI HHHHHCCCCCCHHHH | PubMed | ||
| 150 | Ubiquitination | EISAVCEKGNFNVAH HHHHHHHCCCCCHHH | 19285439 | ||
| 195 | Phosphorylation | NLLRGAVSQRLYILL HHHHHHHHCCEEEEE | 29507054 | ||
| 229 | Phosphorylation | LDKLPQQTGDHAGIK HHCCCCCCCCCCCCC | 24247654 | ||
| 240 | Phosphorylation | AGIKDRVYSNSIYEL CCCCCCCHHCHHHHH | 28450419 | ||
| 241 | Phosphorylation | GIKDRVYSNSIYELL CCCCCCHHCHHHHHH | 28450419 | ||
| 243 | Phosphorylation | KDRVYSNSIYELLEN CCCCHHCHHHHHHHC | 28450419 | ||
| 245 | Phosphorylation | RVYSNSIYELLENGQ CCHHCHHHHHHHCCC | 28450419 | ||
| 289 | Ubiquitination | EDRLEQAKLFCRTLE HHHHHHHHHHHHHHH | - | ||
| 338 | Ubiquitination | RHLRQEEKEEVTVGS HHHHHHHHCCCCCCH | - | ||
| 342 | Phosphorylation | QEEKEEVTVGSLKTS HHHHCCCCCCHHCCC | 29514088 | ||
| 345 | Phosphorylation | KEEVTVGSLKTSAVP HCCCCCCHHCCCCCC | 29514088 | ||
| 353 | Phosphorylation | LKTSAVPSTSTMSQE HCCCCCCCCCCCCCC | 28857561 | ||
| 354 | Phosphorylation | KTSAVPSTSTMSQEP CCCCCCCCCCCCCCC | 28857561 | ||
| 355 | Phosphorylation | TSAVPSTSTMSQEPE CCCCCCCCCCCCCCC | 28348404 | ||
| 356 | Phosphorylation | SAVPSTSTMSQEPEL CCCCCCCCCCCCCCE | 28348404 | ||
| 358 | Phosphorylation | VPSTSTMSQEPELLI CCCCCCCCCCCCEEE | 28348404 | ||
| 366 | Phosphorylation | QEPELLISGMEKPLP CCCCEEECCCCCCCC | 27302953 | ||
| 370 | Ubiquitination | LLISGMEKPLPLRTD EEECCCCCCCCCCCC | - | ||
| 376 | Phosphorylation | EKPLPLRTDFS---- CCCCCCCCCCC---- | 23090842 | ||
| 379 | Phosphorylation | LPLRTDFS------- CCCCCCCC------- | 23090842 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 358 | S | Phosphorylation | Kinase | TBK1 | Q9UHD2 | Uniprot |
| 366 | S | Phosphorylation | Kinase | TBK1 | Q9UHD2 | Uniprot |
| 366 | S | Phosphorylation | Kinase | ULK1 | O75385 | PSP |
| 366 | S | Phosphorylation | Kinase | ULK2 | Q8IYT8 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM32 | Q13049 | PMID:22745133 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF26 | Q9BY78 | PMID:25254379 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM56 | Q9BRZ2 | PMID:23189823 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF5 | Q99942 | PMID:19285439 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of STING_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| 615934 | STING-associated vasculopathy, infantile-onset (SAVI) | |||||
| Kegg Drug | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
