UBXN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBXN1_MOUSE
• UniProt AC: Q922Y1
• Protein Name: UBX domain-containing protein 1
• Gene Name: Ubxn1
• Organism: Mus musculus (Mouse).
• Sequence Length: 297
• Subcellular Localization: Cytoplasm .
• Protein Description: Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling. Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1. Prevents also the activation of NF-kappa-B by associating with CUL1 and thus inhibiting NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-kappa-B. Interacts with the BRCA1-BARD1 heterodimer and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1 leads to the inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol..
• Protein Sequence: MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLSHVLGREPTPSEQVGPEGSGSAAGESRPILTEEERQEQTKRMLELVAQKQREREEREEREALEREKQRRRQGQELSVARQKLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSRSSPPATDPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEEPGQDQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS

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
2	Acetylation	------MAELTALES ------CHHHHHHHH	22.10	-
65	Phosphorylation	HVLGREPTPSEQVGP HHCCCCCCCHHHCCC	34.39	25619855
67	Phosphorylation	LGREPTPSEQVGPEG CCCCCCCHHHCCCCC	43.04	25619855
95	Phosphorylation	EEERQEQTKRMLELV HHHHHHHHHHHHHHH	21.62	18779572
96	Ubiquitination	EERQEQTKRMLELVA HHHHHHHHHHHHHHH	35.19	22790023
105	Ubiquitination	MLELVAQKQREREER HHHHHHHHHHHHHHH	41.40	22790023
132	Phosphorylation	RRQGQELSVARQKLQ HHHHHHHHHHHHHHH	16.99	30635358
137	Ubiquitination	ELSVARQKLQEDEMR HHHHHHHHHHHHHHH	46.73	22790023
154	Ubiquitination	AEERRREKAEELAAR HHHHHHHHHHHHHHH	60.32	22790023
178	Ubiquitination	DKAERAKKYGGSVGS HHHHHHHHHCCCCCC	48.41	-
179	Phosphorylation	KAERAKKYGGSVGSR HHHHHHHHCCCCCCC	26.47	27087446
182	Phosphorylation	RAKKYGGSVGSRSSP HHHHHCCCCCCCCCC	20.95	23684622
185	Phosphorylation	KYGGSVGSRSSPPAT HHCCCCCCCCCCCCC	27.17	25521595
187	Phosphorylation	GGSVGSRSSPPATDP CCCCCCCCCCCCCCC	49.22	25521595
188	Phosphorylation	GSVGSRSSPPATDPG CCCCCCCCCCCCCCC	33.52	27087446
192	O-linked_Glycosylation	SRSSPPATDPGPVPS CCCCCCCCCCCCCCC	48.80	28528544
192	Phosphorylation	SRSSPPATDPGPVPS CCCCCCCCCCCCCCC	48.80	25521595
199	Phosphorylation	TDPGPVPSSPSQEPP CCCCCCCCCCCCCCC	55.93	27087446
200	Phosphorylation	DPGPVPSSPSQEPPT CCCCCCCCCCCCCCC	23.62	25521595
202	Phosphorylation	GPVPSSPSQEPPTKR CCCCCCCCCCCCCCC	49.47	24925903
207	Phosphorylation	SPSQEPPTKREYDQC CCCCCCCCCCCCCCE	54.15	24925903
208	Ubiquitination	PSQEPPTKREYDQCR CCCCCCCCCCCCCEE	49.35	22790023
229	Phosphorylation	DGTSLTQTFRAREQL CCCCHHHHHHHHHHH	15.17	25338131
231	Methylation	TSLTQTFRAREQLAA CCHHHHHHHHHHHHH	35.80	58860227
233	Methylation	LTQTFRAREQLAAVR HHHHHHHHHHHHHHH	28.12	58860235
270	Phosphorylation	GFPRRAFSEADMERP CCCCCCCCHHHCCCH	30.78	30352176
293	Ubiquitination	SAVLIVAKKCPS--- CEEEEEEECCCC---	43.97	-
297	Phosphorylation	IVAKKCPS------- EEEECCCC-------	63.42	21183079

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
200	S	Phosphorylation	Kinase	MAPK12	O08911	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBXN1_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 UBXN1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of UBXN1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND THR-192, ANDMASS SPECTROMETRY.
PubMed: 17242355