dbPTM

TFEB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFEB_HUMAN
UniProt AC	P19484
Protein Name	Transcription factor EB
Gene Name	TFEB
Organism	Homo sapiens (Human).
Sequence Length	476
Subcellular Localization	Cytoplasm . Nucleus . Mainly present in the cytoplasm (PubMed:23434374). Under aberrant lysosomal storage conditions, it translocates from the cytoplasm to the nucleus (PubMed:23434374). In macrophages, translocates into the nucleus upon live S.enter
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	MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASRIGLRMQ -----CCHHHHHHHH	24.11	-
8	Dimethylation	MASRIGLRMQLMREQ CCHHHHHHHHHHHHH	12.94	-
8	Methylation	MASRIGLRMQLMREQ CCHHHHHHHHHHHHH	12.94	54559935
33	Phosphorylation	QQQAVMHYMQQQQQQ HHHHHHHHHHHHHHH	4.40	20068231
50	Phosphorylation	QQLGGPPTPAINTPV HHHCCCCCCCCCCCC	28.61	28348404
55	Phosphorylation	PPTPAINTPVHFQSP CCCCCCCCCCCCCCC	22.15	28348404
61 (in isoform 2)	Phosphorylation	-	38.13	-
61	Phosphorylation	NTPVHFQSPPPVPGE CCCCCCCCCCCCCCC	38.13	20068231
74	Phosphorylation	GEVLKVQSYLENPTS CCEEEEEEHHHCCCC	34.37	25056879
91	Ubiquitination	LQQSQHQKVREYLSE CCHHHHHHHHHHHHH	40.93	-
95	Phosphorylation	QHQKVREYLSETYGN HHHHHHHHHHHHHCC	12.64	-
97	Phosphorylation	QKVREYLSETYGNKF HHHHHHHHHHHCCCC	27.30	28450419
99	Phosphorylation	VREYLSETYGNKFAA HHHHHHHHHCCCCEE	33.09	28450419
100	Phosphorylation	REYLSETYGNKFAAH HHHHHHHHCCCCEEE	18.04	-
109	Phosphorylation	NKFAAHISPAQGSPK CCCEEECCCCCCCCC	12.33	22167270
111	Phosphorylation	FAAHISPAQGSPKPP CEEECCCCCCCCCCC	21.41	27251275
114	Phosphorylation	HISPAQGSPKPPPAA ECCCCCCCCCCCCCC	20.05	22167270
116	Acetylation	SPAQGSPKPPPAASP CCCCCCCCCCCCCCC	72.37	26051181
122	Phosphorylation	PKPPPAASPGVRAGH CCCCCCCCCCCCCCC	25.05	22167270
123	Phosphorylation	KPPPAASPGVRAGHV CCCCCCCCCCCCCCE	40.34	27251275
128	Phosphorylation	ASPGVRAGHVLSSSA CCCCCCCCCEEECCC	10.81	27251275
132	Phosphorylation	VRAGHVLSSSAGNSA CCCCCEEECCCCCCC	22.58	30108239
133	Phosphorylation	RAGHVLSSSAGNSAP CCCCEEECCCCCCCC	21.75	26055452
134	Phosphorylation	AGHVLSSSAGNSAPN CCCEEECCCCCCCCC	36.50	26055452
136	Phosphorylation	HVLSSSAGNSAPNSP CEEECCCCCCCCCCC	30.49	27251275
138	Phosphorylation	LSSSAGNSAPNSPMA EECCCCCCCCCCCCE	44.15	25159151
142	Phosphorylation	AGNSAPNSPMAMLHI CCCCCCCCCCEEEEC	18.26	25159151
147	Phosphorylation	PNSPMAMLHIGSNPE CCCCCEEEECCCCCC	1.61	27251275
151	Phosphorylation	MAMLHIGSNPERELD CEEEECCCCCCHHHH	48.92	30108239
152	Phosphorylation	AMLHIGSNPERELDD EEEECCCCCCHHHHH	36.92	27251275
156	Phosphorylation	IGSNPERELDDVIDN CCCCCCHHHHHHHHH	55.69	27251275
183	Phosphorylation	PEMQMPNTLPLSSSH HHHCCCCCCCCCCCC	24.71	20068231
187	Phosphorylation	MPNTLPLSSSHLNVY CCCCCCCCCCCCEEE	28.05	20068231
188	Phosphorylation	PNTLPLSSSHLNVYS CCCCCCCCCCCEEEC	29.47	20068231
189	Phosphorylation	NTLPLSSSHLNVYSS CCCCCCCCCCEEECC	28.72	20068231
194	Phosphorylation	SSSHLNVYSSDPQVT CCCCCEEECCCCCEE	11.03	20068231
195	Phosphorylation	SSHLNVYSSDPQVTA CCCCEEECCCCCEEH	24.79	20068231
196	Phosphorylation	SHLNVYSSDPQVTAS CCCEEECCCCCEEHH	35.31	20068231
211	Phosphorylation	LVGVTSSSCPADLTQ HEEECCCCCCCCCCH	24.72	22692423
227	Phosphorylation	RELTDAESRALAKER HHCCHHHHHHHHHHH	25.28	20068231
254	Methylation	RRFNINDRIKELGML HHCCHHHHHHHHCCC	37.07	-
274	Ubiquitination	DLDVRWNKGTILKAS CCCCCCCCCHHHHHH	50.93	-
284	Phosphorylation	ILKASVDYIRRMQKD HHHHHHHHHHHHHHH	8.31	27067055
308	Phosphorylation	HSRRLEMTNKQLWLR HHHHHHHHHHHHHHH	29.86	20068231
330	Phosphorylation	ARVHGLPTTSPSGMN HHHHCCCCCCCCCCC	44.97	22167270
331	Phosphorylation	RVHGLPTTSPSGMNM HHHCCCCCCCCCCCH	36.38	22167270
332	Phosphorylation	VHGLPTTSPSGMNMA HHCCCCCCCCCCCHH	21.39	22167270
334	Phosphorylation	GLPTTSPSGMNMAEL CCCCCCCCCCCHHHH	50.90	22167270
346	Phosphorylation	AELAQQVVKQELPSE HHHHHHHHHCCCCCC	4.62	27251275
347	Sumoylation	ELAQQVVKQELPSEE HHHHHHHHCCCCCCC	38.92	-
413	Phosphorylation	EDEGPPGYPEPLAPG CCCCCCCCCCCCCCC	15.36	26074081
423	Phosphorylation	PLAPGHGSPFPSLSK CCCCCCCCCCCCCCH	20.07	22167270
427	Phosphorylation	GHGSPFPSLSKKDLD CCCCCCCCCCHHHHC	45.73	22167270
429	Phosphorylation	GSPFPSLSKKDLDLM CCCCCCCCHHHHCEE	41.83	22167270
437	Phosphorylation	KKDLDLMLLDDSLLP HHHHCEEEECCCCHH	6.53	27251275
441	Phosphorylation	DLMLLDDSLLPLASD CEEEECCCCHHHHCC	31.32	20068231
447	Phosphorylation	DSLLPLASDPLLSTM CCCHHHHCCCCHHHC	47.66	28450419
452	Phosphorylation	LASDPLLSTMSPEAS HHCCCCHHHCCHHHH	29.73	28450419
453	Phosphorylation	ASDPLLSTMSPEASK HCCCCHHHCCHHHHH	22.95	30108239
455	Phosphorylation	DPLLSTMSPEASKAS CCCHHHCCHHHHHHH	21.48	30278072
459	Phosphorylation	STMSPEASKASSRRS HHCCHHHHHHHHCCC	27.39	28450419
462	Phosphorylation	SPEASKASSRRSSFS CHHHHHHHHCCCCCC	28.28	28450419
463	Phosphorylation	PEASKASSRRSSFSM HHHHHHHHCCCCCCC	36.25	28450419
466	Phosphorylation	SKASSRRSSFSMEEG HHHHHCCCCCCCCCC	34.33	25159151
467	Phosphorylation	KASSRRSSFSMEEGD HHHHCCCCCCCCCCC	21.38	28355574
469	Phosphorylation	SSRRSSFSMEEGDVL HHCCCCCCCCCCCCC	27.51	23927012
483	Phosphorylation	L-------------- C--------------		27251275

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
3	S	Phosphorylation	Kinase	MAP4K3	Q8IVH8	GPS
122	S	Phosphorylation	Kinase	MTOR	P42345	PSP
142	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
211	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
467	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATP5J_HUMAN	ATP5J	physical	26496610
IFIT1_HUMAN	IFIT1	physical	26496610
STT3A_HUMAN	STT3A	physical	26496610
TAU_HUMAN	MAPT	physical	26496610
MITF_HUMAN	MITF	physical	26496610
PPM1G_HUMAN	PPM1G	physical	26496610
TFE3_HUMAN	TFE3	physical	26496610
BAG2_HUMAN	BAG2	physical	26496610
LCOR_HUMAN	C10orf12	physical	26496610
FABD_HUMAN	MCAT	physical	26496610
EMAL4_HUMAN	EML4	physical	26496610
TBC14_HUMAN	TBC1D14	physical	26496610
HDAC5_HUMAN	HDAC5	physical	26137861
TFE3_HUMAN	TFE3	physical	28514442
TFEC_HUMAN	TFEC	physical	28514442
TAF9_HUMAN	TAF9	physical	28514442
1433G_HUMAN	YWHAG	physical	28514442
1433Z_HUMAN	YWHAZ	physical	28514442
1433E_HUMAN	YWHAE	physical	28514442
1433B_HUMAN	YWHAB	physical	28514442
GPNMB_HUMAN	GPNMB	physical	28514442
TRI16_HUMAN	TRIM16	physical	27693506

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 TFEB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-114; SER-122AND SER-467, AND MASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-114; SER-122;SER-133; SER-134; SER-138 AND SER-142, AND MASS SPECTROMETRY.	18669648 [Abstract]