dbPTM

TFEB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFEB_MOUSE
UniProt AC	Q9R210
Protein Name	Transcription factor EB
Gene Name	Tfeb
Organism	Mus musculus (Mouse).
Sequence Length	475
Subcellular Localization	Cytoplasm . Nucleus . Mainly present in the cytoplasm. Under aberrant lysosomal storage conditions, it translocates from the cytoplasm to the nucleus. In macrophages, translocates into the nucleus upon live S.enterica infection.
Protein Description	Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF. In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression. It thereby plays a central role in expression of lysosomal genes. Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy. Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer. Plays a role in the signal transduction processes required for normal vascularization of the placenta..
Protein Sequence	MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHVSPAQGSPKPAPAASPGVRAGHVLSTSAGNSAPNSPMAMLHISSNPEKEFDDVIDNIMRLDSVLGYINPEMQMPNTLPLSSSHLNVYSGDPQVTASMVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGVNMAELAQQVVKQELPSEDGPGEALMLGPEVPEPEQMPALPPQAPLPSAAQPQSPFHHLDFSHGLSFGGGGDEGPTGYPDTLGTEHGSPFPNLSKKDLDLMLLDDSLLPLASDPLFSTMSPEASKASSRRSSFSMEEGDVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Methylation	MASRIGLRMQLMREQ CCHHHHHHHHHHHHH	12.94	54559937
8	Dimethylation	MASRIGLRMQLMREQ CCHHHHHHHHHHHHH	12.94	-
73	Phosphorylation	GEVLKVQSYLENPTS CCEEEEEEHHHCCCC	34.37	29514104
80	Phosphorylation	SYLENPTSYHLQQSQ EHHHCCCCHHCCHHH	16.29	29514104
96	Phosphorylation	QKVREYLSETYGNKF HHHHHHHHHHHCCCC	27.30	29514104
98	Phosphorylation	VREYLSETYGNKFAA HHHHHHHHHCCCCEE	33.09	21454597
108	Phosphorylation	NKFAAHVSPAQGSPK CCCEEECCCCCCCCC	12.49	26824392
113	Phosphorylation	HVSPAQGSPKPAPAA ECCCCCCCCCCCCCC	20.05	26824392
121	Phosphorylation	PKPAPAASPGVRAGH CCCCCCCCCCCCCCE	25.05	26824392
131	Phosphorylation	VRAGHVLSTSAGNSA CCCCEEEECCCCCCC	21.16	27087446
132	Phosphorylation	RAGHVLSTSAGNSAP CCCEEEECCCCCCCC	20.59	27087446
133	Phosphorylation	AGHVLSTSAGNSAPN CCEEEECCCCCCCCC	30.70	27087446
137	Phosphorylation	LSTSAGNSAPNSPMA EECCCCCCCCCCCCE	44.15	27087446
141	Phosphorylation	AGNSAPNSPMAMLHI CCCCCCCCCCEEEEC	18.26	27087446
149	Phosphorylation	PMAMLHISSNPEKEF CCEEEECCCCCCHHH	17.20	20531401
150	Phosphorylation	MAMLHISSNPEKEFD CEEEECCCCCCHHHH	56.66	20531401
167	Phosphorylation	IDNIMRLDSVLGYIN HHHHHHHHHHHCCCC	26.74	24719451
172	Phosphorylation	RLDSVLGYINPEMQM HHHHHHCCCCHHHCC	8.05	24719451
180	Phosphorylation	INPEMQMPNTLPLSS CCHHHCCCCCCCCCC	17.48	24719451
182	Phosphorylation	PEMQMPNTLPLSSSH HHHCCCCCCCCCCCC	24.71	22802335
186	Phosphorylation	MPNTLPLSSSHLNVY CCCCCCCCCCCCEEE	28.05	22802335
187	Phosphorylation	PNTLPLSSSHLNVYS CCCCCCCCCCCEEEC	29.47	22802335
188	Phosphorylation	NTLPLSSSHLNVYSG CCCCCCCCCCEEECC	28.72	22802335
193	Phosphorylation	SSSHLNVYSGDPQVT CCCCCEEECCCCCEE	13.08	22802335
194	Phosphorylation	SSHLNVYSGDPQVTA CCCCEEECCCCCEEE	32.22	22802335
200	Phosphorylation	YSGDPQVTASMVGVT ECCCCCEEEHHEEEC	14.04	22802335
202	Phosphorylation	GDPQVTASMVGVTSS CCCCEEEHHEEECCC	12.48	22802335
210	Phosphorylation	MVGVTSSSCPADLTQ HEEECCCCCCCCCCH	24.72	21082442
222	Phosphorylation	LTQKRELTDAESRAL CCHHHHCCHHHHHHH	28.54	23737553
226	Phosphorylation	RELTDAESRALAKER HHCCHHHHHHHHHHH	25.28	26824392
329	Phosphorylation	ARVHGLPTTSPSGVN HHHHCCCCCCCCCCC	44.97	27087446
330	Phosphorylation	RVHGLPTTSPSGVNM HHHCCCCCCCCCCCH	36.38	21082442
331	Phosphorylation	VHGLPTTSPSGVNMA HHCCCCCCCCCCCHH	21.39	27087446
333	Phosphorylation	GLPTTSPSGVNMAEL CCCCCCCCCCCHHHH	55.96	25521595
392	Phosphorylation	QPQSPFHHLDFSHGL CCCCCCCCCCCCCCC	27.72	24719451
422	Phosphorylation	TLGTEHGSPFPNLSK CCCCCCCCCCCCCCH	25.85	-
440	Phosphorylation	DLMLLDDSLLPLASD CEEEECCCCHHHHCC	31.32	-
451	Phosphorylation	LASDPLFSTMSPEAS HHCCCCHHCCCHHHH	30.77	26643407
452	Phosphorylation	ASDPLFSTMSPEASK HCCCCHHCCCHHHHH	17.84	23984901
454	Phosphorylation	DPLFSTMSPEASKAS CCCHHCCCHHHHHHH	21.48	27180971
458	Phosphorylation	STMSPEASKASSRRS HCCCHHHHHHHHCCC	27.39	23649490
461	Phosphorylation	SPEASKASSRRSSFS CHHHHHHHHCCCCCC	28.28	24899341
462	Phosphorylation	PEASKASSRRSSFSM HHHHHHHHCCCCCCC	36.25	24899341
465	Phosphorylation	SKASSRRSSFSMEEG HHHHHCCCCCCCCCC	34.33	27742792
466	Phosphorylation	KASSRRSSFSMEEGD HHHHCCCCCCCCCCC	21.38	25521595
468	Phosphorylation	SSRRSSFSMEEGDVL HHCCCCCCCCCCCCC	27.51	27742792
469	Oxidation	SRRSSFSMEEGDVL- HCCCCCCCCCCCCC-	5.25	17242355

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
141	S	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
210	S	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
461	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
462	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
466	S	Phosphorylation	Kinase	AKT1	P31749	PSP
466	S	Phosphorylation	Kinase	AKT1	P31750	PSP
466	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
468	S	Phosphorylation	Kinase	PRKCB	P05771	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFEB_MOUSE !!

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 TFEB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TFEB_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TFEB_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-121, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-121, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"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-466, AND MASSSPECTROMETRY.	17242355 [Abstract]