TRI13_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI13_MOUSE
• UniProt AC: Q9CYB0
• Protein Name: E3 ubiquitin-protein ligase TRIM13
• Gene Name: Trim13
• Organism: Mus musculus (Mouse).
• Sequence Length: 407
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass membrane protein . Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
• Protein Description: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B..
• Protein Sequence: MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCVTDMQLICGICATRGEHTKHVFSSIEDAYAREKNAFESLFQSFETWRRGDALSRLDTLETNKRKALQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKINTILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPHSNLPTSPLMKNFDTSQWGDIKLVDVDKLSLPQDTGVFTSKIPWYPYLLLMMVVLLGLLIFFGPTVFLEWSPLDELATWKDYLSSFNSYLTKSADFIEQSVFYWEQMTDGFFIFGERVKNVSLVALNNVAEFICKYKLL

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
73	Phosphorylation	VNSLQVNYSLKGIVE CCCEEEEEEHHHHHH	19.27	28576409
179	Phosphorylation	LQLLTKDSDKVKEFF HHHHCCCHHHHHHHH	40.67	-
350	Phosphorylation	ELATWKDYLSSFNSY HHHHHHHHHHHHHHH	12.54	28576409
357	Phosphorylation	YLSSFNSYLTKSADF HHHHHHHHHHHCHHH	21.35	28576409
359	Phosphorylation	SSFNSYLTKSADFIE HHHHHHHHHCHHHHH	18.08	28576409

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

Oops, there are no upstream regulatory protein records of TRI13_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI13_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 TRI13_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IFIH1_MOUSE	Ifih1	physical	25008915

Drug and Disease Associations

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