dbPTM

IFM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IFM3_HUMAN
UniProt AC	Q01628
Protein Name	Interferon-induced transmembrane protein 3
Gene Name	IFITM3
Organism	Homo sapiens (Human).
Sequence Length	133
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 disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. 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), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G 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..
Protein Sequence	MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MNHTVQTFFSP ----CCCCEEECCCC	14.87	29523821
7	Phosphorylation	-MNHTVQTFFSPVNS -CCCCEEECCCCCCC	23.47	23663014
10	Phosphorylation	HTVQTFFSPVNSGQP CCEEECCCCCCCCCC	24.60	28355574
14	Phosphorylation	TFFSPVNSGQPPNYE ECCCCCCCCCCCCHH	38.75	25159151
20	Phosphorylation	NSGQPPNYEMLKEEH CCCCCCCHHHHHHHH	14.43	25627689
24	Ubiquitination	PPNYEMLKEEHEVAV CCCHHHHHHHHEEEE	60.80	22511783
42	Phosphorylation	PHNPAPPTSTVIHIR CCCCCCCCCEEEEEE	35.65	28348404
43	Phosphorylation	HNPAPPTSTVIHIRS CCCCCCCCEEEEEEC	26.84	28348404
44	Phosphorylation	NPAPPTSTVIHIRSE CCCCCCCEEEEEECC	26.42	24173317
52	Phosphorylation	VIHIRSETSVPDHVV EEEEECCCCCCCHHH	35.95	-
71	S-palmitoylation	NTLFMNPCCLGFIAF HHHHCCHHHHHHHHH	2.25	27044110
72	S-palmitoylation	TLFMNPCCLGFIAFA HHHCCHHHHHHHHHH	4.37	27044110
83	Ubiquitination	IAFAYSVKSRDRKMV HHHHHHCCCCCCCCC	33.56	83
88	Ubiquitination	SVKSRDRKMVGDVTG HCCCCCCCCCCCCCH	42.07	27667366
88	Ubiquitination	SVKSRDRKMVGDVTG HCCCCCCCCCCCCCH	42.07	21890473
94	Phosphorylation	RKMVGDVTGAQAYAS CCCCCCCCHHHHHHH	31.38	28152594
99	Phosphorylation	DVTGAQAYASTAKCL CCCHHHHHHHHHHHH	6.76	28152594
101	Phosphorylation	TGAQAYASTAKCLNI CHHHHHHHHHHHHHH	19.07	28152594
102	Phosphorylation	GAQAYASTAKCLNIW HHHHHHHHHHHHHHH	23.20	28152594
104	Ubiquitination	QAYASTAKCLNIWAL HHHHHHHHHHHHHHH	39.07	2251178
105	S-palmitoylation	AYASTAKCLNIWALI HHHHHHHHHHHHHHH	3.05	27044110

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
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:26263374

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
24	K	ubiquitylation	22511783
Lys-24 is the most prevalent ubiquitination site.
48	K	ubiquitylation	22511783
Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
63	K	ubiquitylation	22511783
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of IFM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAMPT_HUMAN	NAMPT	physical	18486613
FYN_HUMAN	FYN	physical	23055554
NEDD4_HUMAN	NEDD4	physical	26263374

Drug and Disease Associations

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

Regulatory Network of IFM3_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"S-palmitoylation and ubiquitination differentially regulateinterferon-induced transmembrane protein 3 (IFITM3)-mediatedresistance to influenza virus."; Yount J.S., Karssemeijer R.A., Hang H.C.; J. Biol. Chem. 0:0-0(2012). Cited for: UBIQUITINATION AT LYS-24; LYS-83; LYS-88 AND LYS-104, PALMITOYLATION,TOPOLOGY, ABSENCE OF GLYCOSYLATION, AND SUBCELLULAR LOCATION.	22511783 [Abstract]
"Palmitoylome profiling reveals S-palmitoylation-dependent antiviralactivity of IFITM3."; Yount J.S., Moltedo B., Yang Y.Y., Charron G., Moran T.M., Lopez C.B.,Hang H.C.; Nat. Chem. Biol. 6:610-614(2010). Cited for: PALMITOYLATION AT CYS-71; CYS-72 AND CYS-105.	20601941 [Abstract]
Ubiquitylation
Reference	PubMed
"S-palmitoylation and ubiquitination differentially regulateinterferon-induced transmembrane protein 3 (IFITM3)-mediatedresistance to influenza virus."; Yount J.S., Karssemeijer R.A., Hang H.C.; J. Biol. Chem. 0:0-0(2012). Cited for: UBIQUITINATION AT LYS-24; LYS-83; LYS-88 AND LYS-104, PALMITOYLATION,TOPOLOGY, ABSENCE OF GLYCOSYLATION, AND SUBCELLULAR LOCATION.	22511783 [Abstract]

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