MUL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MUL1_MOUSE
• UniProt AC: Q8VCM5
• Protein Name: Mitochondrial ubiquitin ligase activator of NFKB 1
• Gene Name: Mul1
• Organism: Mus musculus (Mouse).
• Sequence Length: 352
• Subcellular Localization: Mitochondrion outer membrane; Multi-pass membrane protein. Peroxisome. Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome..
• Protein Description: Exhibits weak E3 ubiquitin-protein ligase activity (By similarity). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (By similarity). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (By similarity). Plays a role in the control of mitochondrial morphology by promoting mitchondrial fragmentation, and influences mitochondrial localization (By similarity). Likely to promote mitchondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway. [PubMed: 24898855 May also be involved in the sumoylation of the membrane fission protein DNM1L (By similarity Inhibits cell growth (By similarity When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (By similarity Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (By similarity Can mediate DDX58 sumoylation and disrupt its polyubiquitination (By similarity]
• Protein Sequence: MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELKGAKKIHLGEDLKGILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLSLQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETVYEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQGMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFFILRKQYLHRQERLRQQQLQEEFLEHEAQLLSQASPEDRESLKSACVVCLSNFKSCVFLECGHVCSCRQCYLALPEPKRCPICRREITRVIPLYNS

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
288	Phosphorylation	EHEAQLLSQASPEDR HHHHHHHHHCCHHHH	32.09	19060867
291	Phosphorylation	AQLLSQASPEDRESL HHHHHHCCHHHHHHH	22.61	22817900
297	Phosphorylation	ASPEDRESLKSACVV CCHHHHHHHHHHHHH	41.83	29899451

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

Oops, there are no upstream regulatory protein records of MUL1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MUL1_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 MUL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NR6A1_MOUSE	Nr6a1	physical	18082624

Drug and Disease Associations

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