TRI56_HUMAN - dbPTM
TRI56_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI56_HUMAN
UniProt AC Q9BRZ2
Protein Name E3 ubiquitin-protein ligase TRIM56
Gene Name TRIM56
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity. [PubMed: 21289118 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 (By similarity 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. Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus]
Protein Sequence MVSHGSSPSLLEALSSDFLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASFKTNFFVNGLLDLVKARACGDLRAGKPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWAPGPAPCLLPQLELHPGLLDKNCHLLRLSFEEQQPQKDGGKDGAGTQGGEESQSRREDEPKTERQGGVQPQAGDGAQTPKEEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHRGGRPNKKKKFKGRLKSISREPSPALGPNLDGSGLLPRPIFYCSFPTRMPGDKRSPRITGLCPFGPREILVADEQNRALKRFSLNGDYKGTVPVPEGCSPCSVAALQSAVAFSASARLYLINPNGEVQWRRALSLSQASHAVAALPSGDRVAVSVAGHVEVYNMEGSLATRFIPGGKASRGLRALVFLTTSPQGHFVGSDWQQNSVVICDGLGQVVGEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHIFRVRSPDS
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
3Phosphorylation-----MVSHGSSPSL
-----CCCCCCCHHH		22.3428464451
6Phosphorylation--MVSHGSSPSLLEA
--CCCCCCCHHHHHH		33.3825159151
7Phosphorylation-MVSHGSSPSLLEAL
-CCCCCCCHHHHHHH		24.0928464451
9PhosphorylationVSHGSSPSLLEALSS
CCCCCCHHHHHHHCC		47.7528464451
15PhosphorylationPSLLEALSSDFLACK
HHHHHHHCCCHHHHH		34.6026552605
16PhosphorylationSLLEALSSDFLACKI
HHHHHHCCCHHHHHH		32.9826074081
62PhosphorylationRCPECRETVPVPPEG
ECCCCCCCCCCCCCC		15.68-
72PhosphorylationVPPEGVASFKTNFFV
CCCCCCCCCCCCCCH		25.5224719451
87UbiquitinationNGLLDLVKARACGDL
HCHHHHHHHHHCCCC		39.1823000965
98UbiquitinationCGDLRAGKPACALCP
CCCCCCCCCEEEECC		28.58-
117PhosphorylationTSTGGPATARCLDCA
CCCCCHHHHHHHHCH		20.1225137130
157PhosphorylationVGYRAGWYDEEARER
HHHCCCCCCHHHHHH		16.7427642862
253PhosphorylationEQAARVGTQVEEAAE
HHHHHHCCHHHHHHH		26.9521406692
270UbiquitinationLRALLAQKQEVLGQL
HHHHHHHHHHHHHHH		42.7023000965
369PhosphorylationNCHLLRLSFEEQQPQ
CCEEEEEECCCCCCC		24.9520873877
377UbiquitinationFEEQQPQKDGGKDGA
CCCCCCCCCCCCCCC		66.0924816145
381UbiquitinationQPQKDGGKDGAGTQG
CCCCCCCCCCCCCCC		59.5233845483
392PhosphorylationGTQGGEESQSRREDE
CCCCCCHHHCCCCCC		29.2024275569
418PhosphorylationQAGDGAQTPKEEKAQ
CCCCCCCCCHHHHCH		35.4829255136
426PhosphorylationPKEEKAQTTREEGAQ
CHHHHCHHCHHHHCH		32.4523186163
427PhosphorylationKEEKAQTTREEGAQT
HHHHCHHCHHHHCHH		24.8124505115
434PhosphorylationTREEGAQTLEEDRAQ
CHHHHCHHHHHHHCC		35.2922167270
442PhosphorylationLEEDRAQTPHEDGGP
HHHHHCCCCCCCCCC		26.1530266825
469PhosphorylationKFKGRLKSISREPSP
HHCCHHHHCCCCCCC		30.3229255136
471PhosphorylationKGRLKSISREPSPAL
CCHHHHCCCCCCCCC		37.3729255136
475PhosphorylationKSISREPSPALGPNL
HHCCCCCCCCCCCCC		20.3229255136
485PhosphorylationLGPNLDGSGLLPRPI
CCCCCCCCCCCCCCE		26.4030266825
494PhosphorylationLLPRPIFYCSFPTRM
CCCCCEEEEECCCCC		6.4723090842
496PhosphorylationPRPIFYCSFPTRMPG
CCCEEEEECCCCCCC		23.9223090842
499PhosphorylationIFYCSFPTRMPGDKR
EEEEECCCCCCCCCC		37.2722115753
554PhosphorylationPEGCSPCSVAALQSA
CCCCCHHHHHHHHHH		20.4132142685
567PhosphorylationSAVAFSASARLYLIN
HHHHHCCCCEEEEEC		16.8432142685
688UbiquitinationPGSVSVDKKGYIFLT
CCCEEECCCCEEEEE		46.0429967540
710PhosphorylationVILDPKGSLLGDFLT
EEECCCCCCHHHHHH		26.9222817900
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI56_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STING_HUMANTMEM173physical
21074459
TCAM1_HUMANTICAM1physical
22948160
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI56_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418; THR-442 ANDSER-475, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; SER-471 ANDSER-475, AND MASS SPECTROMETRY.

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