RSAD2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RSAD2_MOUSE
• UniProt AC: Q8CBB9
• Protein Name: Radical S-adenosyl methionine domain-containing protein 2
• Gene Name: Rsad2 {ECO:0000312|MGI:MGI:1929628}
• Organism: Mus musculus (Mouse).
• Sequence Length: 362
• Subcellular Localization: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet.
• Protein Description: Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of viruses, including west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus and vesicular stomatitis virus (VSV). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphosphate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins..
• Protein Sequence: MGMLVPTALAARLLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEDGNSTQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW

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
58	Phosphorylation	VRGEPEDTQETQEDG CCCCCCCCCCCCCCC	27.00	30635358
61	Phosphorylation	EPEDTQETQEDGNST CCCCCCCCCCCCCCC	27.69	30635358
67	Phosphorylation	ETQEDGNSTQPTTPV CCCCCCCCCCCCCCE	33.67	30635358
68	Phosphorylation	TQEDGNSTQPTTPVS CCCCCCCCCCCCCEE	42.44	30635358
71	Phosphorylation	DGNSTQPTTPVSVNY CCCCCCCCCCEEEEE	33.64	30635358
72	Phosphorylation	GNSTQPTTPVSVNYH CCCCCCCCCEEEEEE	28.51	25159016
75	Phosphorylation	TQPTTPVSVNYHFTR CCCCCCEEEEEEEEC	13.07	25159016
78	Phosphorylation	TTPVSVNYHFTRQCN CCCEEEEEEEECCCC	8.99	30635358
81	Phosphorylation	VSVNYHFTRQCNYKC EEEEEEEECCCCCEE	13.40	30635358
198	Acetylation	LIGRGQGKKNHVENL HHHCCCCCHHHHHHH	42.38	-
199	Ubiquitination	IGRGQGKKNHVENLQ HHCCCCCHHHHHHHH	60.14	-
242	Phosphorylation	NEHIKALSPVRWKVF HHHHHHHCHHHHHHE	26.64	24719451
285	Ubiquitination	ETFLERHKEVSCLVP HHHHHHHHCCEEECC	67.06	-
299	Ubiquitination	PESNQKMKDSYLILD CCCCHHHCCCEEEHH	51.03	-
354	Phosphorylation	RGGKYVWSKADLKLD ECCEEEEECCCCCCC	14.12	22817900

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

Oops, there are no upstream regulatory protein records of RSAD2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
198	K	Acetylation	HAT1-mediated acetylation of Lys-198 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation.	-
198	K	ubiquitylation	HAT1-mediated acetylation of Lys-198 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation.	-
207	K	ubiquitylation	'Lys-6'-linked polyubiquitination at Lys-207 leads to RSAD2 protein degradation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RSAD2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRAK1_MOUSE	Irak1	physical	21435586
TRAF6_MOUSE	Traf6	physical	21435586
TRAF6_HUMAN	TRAF6	physical	21435586
IRAK1_HUMAN	IRAK1	physical	21435586
IRF7_MOUSE	Irf7	physical	21435586

Drug and Disease Associations

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