IFM3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IFM3_MOUSE
• UniProt AC: Q9CQW9
• Protein Name: Interferon-induced transmembrane protein 3
• Gene Name: Ifitm3
• Organism: Mus musculus (Mouse).
• Sequence Length: 137
• Subcellular Localization: Cell membrane; Single-pass type II membrane protein. Late endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein.
• Protein Description: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV) and human immunodeficiency virus type 1 (HIV-1). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. Involved in initiating germ cell competence and specification, and in the demarcation of PGCs from their somatic neighbors..
• Protein Sequence: MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT

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
4	Phosphorylation	----MNHTSQAFITA ----CCCCCCHHHHH	19.96	25619855
5	Phosphorylation	---MNHTSQAFITAA ---CCCCCCHHHHHH	16.38	25619855
13	Phosphorylation	QAFITAASGGQPPNY CHHHHHHCCCCCCCH	40.78	29514104
20	Phosphorylation	SGGQPPNYERIKEEY CCCCCCCHHHHHHHH	16.62	26824392
24	Ubiquitination	PPNYERIKEEYEVAE CCCHHHHHHHHHHHH	51.19	22790023
24	Acetylation	PPNYERIKEEYEVAE CCCHHHHHHHHHHHH	51.19	23806337
27	Phosphorylation	YERIKEEYEVAEMGA HHHHHHHHHHHHCCC	19.45	26824392
38	Phosphorylation	EMGAPHGSASVRTTV HCCCCCCCCCCEEEE	17.84	22942356
40	Phosphorylation	GAPHGSASVRTTVIN CCCCCCCCCEEEEEC	17.52	26824392
43	Phosphorylation	HGSASVRTTVINMPR CCCCCCEEEEECCCC	24.22	25266776
44	Phosphorylation	GSASVRTTVINMPRE CCCCCEEEEECCCCC	14.61	25266776
71	S-palmitoylation	NTLFMNFCCLGFIAY HHHHHHHHHHHHHHH	1.27	22511783
72	S-palmitoylation	TLFMNFCCLGFIAYA HHHHHHHHHHHHHHH	3.49	22511783
88	Ubiquitination	SVKSRDRKMVGDVTG HCCCCCCCCCCCCCH	42.07	22790023
94	Phosphorylation	RKMVGDVTGAQAYAS CCCCCCCCHHHHHHH	31.38	30482847
99	Phosphorylation	DVTGAQAYASTAKCL CCCHHHHHHHHHHHH	6.76	25338131
101	Phosphorylation	TGAQAYASTAKCLNI CHHHHHHHHHHHHCH	19.07	29899451
105	S-palmitoylation	AYASTAKCLNISTLV HHHHHHHHHCHHHHH	3.05	22511783

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
20	Y	Phosphorylation	Kinase	FYN	P06241	PSP
27	Y	Phosphorylation	Kinase	FYN	P06241	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
24	K	ubiquitylation	Lys-24 is the most prevalent ubiquitination site (By similarity).	-
48	K	ubiquitylation	Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.	-
63	K	ubiquitylation	Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IFM3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VATO_MOUSE	Atp6v0b	physical	22467717

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, AND MASSSPECTROMETRY.
PubMed: 19144319