STING_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STING_MOUSE
• UniProt AC: Q3TBT3
• Protein Name: Stimulator of interferon genes protein {ECO:0000303|PubMed:18724357, ECO:0000303|PubMed:19776740}
• Gene Name: Tmem173
• Organism: Mus musculus (Mouse).
• Sequence Length: 378
• 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. 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]
• Protein Sequence: MPYSNLHPAIPRPRGHRSKYVALIFLVASLMILWVAKDPPNHTLKYLALHLASHELGLLLKNLCCLAEELCHVQSRYQGSYWKAVRACLGCPIHCMAMILLSSYFYFLQNTADIYLSWMFGLLVLYKSLSMLLGLQSLTPAEVSAVCEEKKLNVAHGLAWSYYIGYLRLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDNLSVVDPNIRFRDMLPQQNIDRAGIKNRVYSNSVYEILENGQPAGVCILEYATPLQTLFAMSQDAKAGFSREDRLEQAKLFCRTLEEILEDVPESRNNCRLIVYQEPTDGNSFSLSQEVLRHIRQEEKEEVTMNAPMTSVAPPPSVLSQEPRLLISGMDQPLPLRTDLI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
88	S-palmitoylation	YWKAVRACLGCPIHC HHHHHHHHHCCHHHH		29973723
91	S-palmitoylation	AVRACLGCPIHCMAM HHHHHHCCHHHHHHH		29973723
150	Ubiquitination	VSAVCEEKKLNVAHG HHHHHHHHCCCHHHH		-
337	Sumoylation	RHIRQEEKEEVTMNA HHHHHHHHHHCCCCC		-
357	Phosphorylation	APPPSVLSQEPRLLI CCCCCHHCCCCCEEE		-
365	Phosphorylation	QEPRLLISGMDQPLP CCCCEEECCCCCCCC		25159016

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
357	S	Phosphorylation	Kinase	TBK1	Q9WUN2	Uniprot
365	S	Phosphorylation	Kinase	TBK1	Q9WUN2	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Rnf5	O35445	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Trim56	Q80VI1	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
150	K	ubiquitylation	'Lys-11'-linked polyubiquitination at Lys-150 by RNF26 leads to stabilize STING1: it protects STING1 from RNF5-mediated 'Lys-48'-linked polyubiquitination (By similarity).	29496741
150	K	ubiquitylation	'Lys-48'-linked polyubiquitination at Lys-150 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation (By similarity).	29496741
150	K	ubiquitylation	'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 (By similarity).	29496741
365	S	Phosphorylation	Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-365 in the pLxIS motif.	25636800

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of STING_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of STING_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.