TRI25_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI25_MOUSE
• UniProt AC: Q61510
• Protein Name: E3 ubiquitin/ISG15 ligase TRIM25
• Gene Name: Trim25
• Organism: Mus musculus (Mouse).
• Sequence Length: 634
• Subcellular Localization: Cytoplasm . Colocalized with DDX58 at cytoplasmic perinuclear bodies.
• Protein Description: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3..
• Protein Sequence: MAELNPLAEELSCSVCLELFKEPVTTPCGHNFCMSCLDETWVVQGPPYRCPQCRKVYQVRPQLQKNTVMCAVVEQFLQAEQARTPVDDWTPPARFSASSAATQVACDHCLTEIAVKTCLVCMASFCQEHLRPHFDSPAFQDHPLQSPIRDLLRRKCTQHNRLRELFCPEHGECICHICLVEHKTCSPTTLSQASADLEYKLRNKLTIMHSHINGATKALEDVRSKQQCVQDSMKRKMEQLRQEYMEMKAVIDAAETSSLRKLKEEEKRVYGKFDTIYQVLVKKKSEMQKLKAEVELIMDKGDEFEFLEKAAKLQGESTKPVYIPKIDLDHDLIMGIYQGAADLKSELKHSIKKLQKKSEEHNGSGNKGDQTQSTFKPVQPSKKTIQEKKTKKTPVAPGPPSHFSPNKLPTFGAPGQSLDSKATSPDAAPKASAAQPDSVGVKAKVLENFLTKSRTELLEYFVKVIFDYNTAHNKVSLSNKYTTASVSDGLQHYRSHPQRFTYCSQVLGLHCYKNGIHYWEVELQKNNFCGVGICYGSMERQGPESRLGRNPNSWCVEWFNNKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVTEKVHLMYKFKVDFTEALYPAFWVFSAGTTLSICSK

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
70	S-palmitoylation	LQKNTVMCAVVEQFL HCCCHHHHHHHHHHH	1.95	28526873
84	Phosphorylation	LQAEQARTPVDDWTP HHHHHCCCCCCCCCC	30.58	27180971
90	Phosphorylation	RTPVDDWTPPARFSA CCCCCCCCCCCCCCC	26.79	26745281
99	Phosphorylation	PARFSASSAATQVAC CCCCCCCHHHHHHHH	22.95	-
116	Ubiquitination	CLTEIAVKTCLVCMA HHHHHHHHHHHHHHH	25.21	-
184	Phosphorylation	ICLVEHKTCSPTTLS EEEEECCCCCCCCHH	21.81	26643407
186	Phosphorylation	LVEHKTCSPTTLSQA EEECCCCCCCCHHHH	30.43	26643407
194	Phosphorylation	PTTLSQASADLEYKL CCCHHHHCCCHHHHH	18.06	21183079
200	Ubiquitination	ASADLEYKLRNKLTI HCCCHHHHHHHCHHH	31.43	22790023
225	Ubiquitination	ALEDVRSKQQCVQDS HHHHHHHHHHHHHHH	33.55	22790023
228	Glutathionylation	DVRSKQQCVQDSMKR HHHHHHHHHHHHHHH	2.48	24333276
234	Ubiquitination	QCVQDSMKRKMEQLR HHHHHHHHHHHHHHH	53.47	22790023
257	Phosphorylation	VIDAAETSSLRKLKE HHHHHHHHHHHHHHH	20.91	30352176
258	Phosphorylation	IDAAETSSLRKLKEE HHHHHHHHHHHHHHH	39.34	30352176
270	Phosphorylation	KEEEKRVYGKFDTIY HHHHHHHHCCHHHHH	20.73	25367039
272	Acetylation	EEKRVYGKFDTIYQV HHHHHHCCHHHHHHH	23.52	-
275	Phosphorylation	RVYGKFDTIYQVLVK HHHCCHHHHHHHHHH	25.39	25367039
277	Phosphorylation	YGKFDTIYQVLVKKK HCCHHHHHHHHHHCH	8.48	22817900
282	Ubiquitination	TIYQVLVKKKSEMQK HHHHHHHHCHHHHHH	50.77	22790023
309	Ubiquitination	DEFEFLEKAAKLQGE CHHHHHHHHHHHCCC	56.65	22790023
312	Ubiquitination	EFLEKAAKLQGESTK HHHHHHHHHCCCCCC	46.32	22790023
319	Ubiquitination	KLQGESTKPVYIPKI HHCCCCCCCEEEECC	41.59	22790023
344	Ubiquitination	YQGAADLKSELKHSI HHHHHHHHHHHHHHH	42.29	-
350	Phosphorylation	LKSELKHSIKKLQKK HHHHHHHHHHHHHHH	34.22	29176673
358	Phosphorylation	IKKLQKKSEEHNGSG HHHHHHHHHHCCCCC	56.08	28576409
376	Ubiquitination	DQTQSTFKPVQPSKK CCCCCCCCCCCCCCC	44.35	22790023
381	Phosphorylation	TFKPVQPSKKTIQEK CCCCCCCCCCCCCCC	29.68	-
382	Ubiquitination	FKPVQPSKKTIQEKK CCCCCCCCCCCCCCC	61.70	22790023
383	Acetylation	KPVQPSKKTIQEKKT CCCCCCCCCCCCCCC	56.02	22902405
388	Acetylation	SKKTIQEKKTKKTPV CCCCCCCCCCCCCCC	49.74	22902405
393	Phosphorylation	QEKKTKKTPVAPGPP CCCCCCCCCCCCCCC	25.26	27087446
401	Phosphorylation	PVAPGPPSHFSPNKL CCCCCCCCCCCCCCC	40.05	23375375
404	Phosphorylation	PGPPSHFSPNKLPTF CCCCCCCCCCCCCCC	23.34	27087446
407	Ubiquitination	PSHFSPNKLPTFGAP CCCCCCCCCCCCCCC	60.26	22790023
410	Phosphorylation	FSPNKLPTFGAPGQS CCCCCCCCCCCCCCC	45.17	26745281
417	Phosphorylation	TFGAPGQSLDSKATS CCCCCCCCCCCCCCC	39.81	26643407
420	Phosphorylation	APGQSLDSKATSPDA CCCCCCCCCCCCCCC	29.50	25777480
421	Ubiquitination	PGQSLDSKATSPDAA CCCCCCCCCCCCCCC	56.18	22790023
423	Phosphorylation	QSLDSKATSPDAAPK CCCCCCCCCCCCCCC	44.52	22324799
424	Phosphorylation	SLDSKATSPDAAPKA CCCCCCCCCCCCCCC	26.16	25521595
430	Ubiquitination	TSPDAAPKASAAQPD CCCCCCCCCCCCCCC	50.69	22790023
442	Ubiquitination	QPDSVGVKAKVLENF CCCCHHHHHHHHHHH	36.24	22790023
444	Ubiquitination	DSVGVKAKVLENFLT CCHHHHHHHHHHHHC	41.45	22790023
480	Ubiquitination	NKVSLSNKYTTASVS CEECCCCCCCCEECC	40.37	-
480	Malonylation	NKVSLSNKYTTASVS CEECCCCCCCCEECC	40.37	26320211
518	Phosphorylation	CYKNGIHYWEVELQK EECCCEEEEEEEECC	11.01	30352176
555	S-palmitoylation	GRNPNSWCVEWFNNK CCCCCCHHHHHHCCC	1.67	28526873
572	Acetylation	AWHNNVEKTLPSTKA HHHHCHHHHCCCCCC	51.59	-

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

Oops, there are no upstream regulatory protein records of TRI25_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI25_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRI25_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDX58_MOUSE	Ddx58	physical	24015671

Drug and Disease Associations

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