TRI56_MOUSE - dbPTM
TRI56_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI56_MOUSE
UniProt AC Q80VI1
Protein Name E3 ubiquitin-protein ligase TRIM56
Gene Name Trim56
Organism Mus musculus (Mouse).
Sequence Length 734
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity. In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets TMEM173/STING to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta. Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity)..
Protein Sequence MNSKVSSPTLLEALSSDFLACKICLEQLHTPKTLPCLHTYCQDCLAQLDIGGQVRCPECREIVPVPAEGVAAFKTNFFVNGLLDLVKARAPGDVHSGKPTCALCPLVGGKSSGGPATARCLDCADDLCQACADGHRCSRQTHKHRVVDLVGYRAGWYDEEARERQASQCPQHPGEALCFLCQPCSQLLCKDCRLGPHIDHPCLPLAEAVRSRKPGLEELLAGVDSNLVELEATRVAEKEALALLREQAASVGTQVEEAAERILKSLLAQKQEVLGQLRALVEAAEEATRERLTKIERQEQVAKAAAAFARRVLSLGLEAEILSLEGAITQRLRQLQDAPWTSGPTRCVLPQLELHPGLEDKNCHLLRLIFEEPKQSPKDSGKGGAGTQGGDEAQGQGDDRTKIGKQGGAQPLTPKEGKDQNPQEDDGVFIERGNRPNKKKKCKGRGKSVSREPSPILRPNLEGSGLLPRPVFSWSFPTRMPGDKRSPRITGLCPYGPQEILVADEQNRVLKRFSLNGDYKGTVQVPEGCSPCSVAALQNAVAFSANAKLYLVSPDGEIQWRRSLSLTQSSHAVAAMPCGDRVAVSVAGHVEVYKKDGSLATRFIPGGKASRGQRALVFLTTSPQGNFVGSDWQQNSVVFCDGLGQVIWEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGKYLVVSLSNGTIHVFRVRFPDS
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 Orthologous
Protein Cluster
6Phosphorylation--MNSKVSSPTLLEA
--CCCCCCCHHHHHH
34.0426745281
7Phosphorylation-MNSKVSSPTLLEAL
-CCCCCCCHHHHHHH
25.5426745281
9PhosphorylationNSKVSSPTLLEALSS
CCCCCCHHHHHHHCC
46.0226745281
15PhosphorylationPTLLEALSSDFLACK
HHHHHHHCCCHHHHH
34.6025777480
16PhosphorylationTLLEALSSDFLACKI
HHHHHHCCCHHHHHH
32.9825777480
87UbiquitinationNGLLDLVKARAPGDV
HCHHHHHHHCCCCCC
39.1822790023
110AcetylationLCPLVGGKSSGGPAT
EECCCCCCCCCCCCC
35.2023806337
270UbiquitinationLKSLLAQKQEVLGQL
HHHHHHHHHHHHHHH
42.7022790023
314PhosphorylationAFARRVLSLGLEAEI
HHHHHHHHHCHHHHH
19.9617203969
323PhosphorylationGLEAEILSLEGAITQ
CHHHHHHHHHHHHHH
30.00-
329PhosphorylationLSLEGAITQRLRQLQ
HHHHHHHHHHHHHHH
13.70-
374UbiquitinationRLIFEEPKQSPKDSG
HHHHCCCCCCCCCCC
67.6922790023
376PhosphorylationIFEEPKQSPKDSGKG
HHCCCCCCCCCCCCC
39.7926824392
380PhosphorylationPKQSPKDSGKGGAGT
CCCCCCCCCCCCCCC
48.8324068923
405UbiquitinationDDRTKIGKQGGAQPL
CCCCCCCCCCCCCCC
49.6022790023
413PhosphorylationQGGAQPLTPKEGKDQ
CCCCCCCCCCCCCCC
38.7124453211
448PhosphorylationKCKGRGKSVSREPSP
CCCCCCCCCCCCCCC
28.3126824392
450PhosphorylationKGRGKSVSREPSPIL
CCCCCCCCCCCCCCC
37.7126824392
454PhosphorylationKSVSREPSPILRPNL
CCCCCCCCCCCCCCC
21.5926824392
464PhosphorylationLRPNLEGSGLLPRPV
CCCCCCCCCCCCCCE
19.5226643407

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

Oops, there are no upstream regulatory protein records of TRI56_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI56_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 TRI56_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TRI56_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI56_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-450 ANDSER-454, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASSSPECTROMETRY.

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