dbPTM

TFE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFE2_HUMAN
UniProt AC	P15923
Protein Name	Transcription factor E2-alpha
Gene Name	TCF3
Organism	Homo sapiens (Human).
Sequence Length	654
Subcellular Localization	Nucleus.
Protein Description	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region..
Protein Sequence	MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGSRGTTAGSSGDALGKALASIYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	QRMAPVGTDKELSDL CCCCCCCCCHHHHHH	44.10	23403867
23	Phosphorylation	LSDLLDFSMMFPLPV HHHHCCHHHCCCCCC	14.70	22210691
34	Acetylation	PLPVTNGKGRPASLA CCCCCCCCCCCHHHC	54.54	22207202
39	Phosphorylation	NGKGRPASLAGAQFG CCCCCCHHHCCCCCC	22.80	25159151
39 (in isoform 3)	Phosphorylation	-	22.80	29507054
48 (in isoform 3)	Phosphorylation	-	40.35	25627689
51 (in isoform 3)	Phosphorylation	-	56.34	29507054
55	Phosphorylation	SGLEDRPSSGSWGSG CCCCCCCCCCCCCCC	48.50	23401153
57 (in isoform 3)	Phosphorylation	-	31.58	25159151
102	Phosphorylation	GPGLGGKSGERGAYA CCCCCCCCCCCCCCC	49.51	29449344
105	Methylation	LGGKSGERGAYASFG CCCCCCCCCCCCCCC	38.27	-
108	Phosphorylation	KSGERGAYASFGRDA CCCCCCCCCCCCCCC	12.95	28796482
110	Phosphorylation	GERGAYASFGRDAGV CCCCCCCCCCCCCCC	18.63	28555341
121	Phosphorylation	DAGVGGLTQAGFLSG CCCCCCCHHHCHHCC	21.46	28464451
127	Phosphorylation	LTQAGFLSGELALNS CHHHCHHCCEEECCC	28.14	23403867
134	Phosphorylation	SGELALNSPGPLSPS CCEEECCCCCCCCCC	31.89	26055452
139	Phosphorylation	LNSPGPLSPSGMKGT CCCCCCCCCCCCCCC	21.83	30278072
141	Phosphorylation	SPGPLSPSGMKGTSQ CCCCCCCCCCCCCCC	48.41	30278072
146	Phosphorylation	SPSGMKGTSQYYPSY CCCCCCCCCCCCCCC	13.72	21945579
147	Phosphorylation	PSGMKGTSQYYPSYS CCCCCCCCCCCCCCC	25.50	21945579
149	Phosphorylation	GMKGTSQYYPSYSGS CCCCCCCCCCCCCCC	19.67	21945579
150	Phosphorylation	MKGTSQYYPSYSGSS CCCCCCCCCCCCCCC	4.32	21945579
152	Phosphorylation	GTSQYYPSYSGSSRR CCCCCCCCCCCCCCC	18.79	21945579
153	Phosphorylation	TSQYYPSYSGSSRRR CCCCCCCCCCCCCCC	16.73	26074081
154	Phosphorylation	SQYYPSYSGSSRRRA CCCCCCCCCCCCCCC	36.21	21945579
156	Phosphorylation	YYPSYSGSSRRRAAD CCCCCCCCCCCCCCC	18.09	25262027
157	Phosphorylation	YPSYSGSSRRRAADG CCCCCCCCCCCCCCC	33.07	21945579
165	Phosphorylation	RRRAADGSLDTQPKK CCCCCCCCCCCCCCC	24.50	26074081
168	Phosphorylation	AADGSLDTQPKKVRK CCCCCCCCCCCCCCC	52.65	27794612
171	Acetylation	GSLDTQPKKVRKVPP CCCCCCCCCCCCCCC	54.83	30588339
182	Phosphorylation	KVPPGLPSSVYPPSS CCCCCCCCCCCCCCC	37.16	26552605
183	Phosphorylation	VPPGLPSSVYPPSSG CCCCCCCCCCCCCCC	24.59	26552605
185	Phosphorylation	PGLPSSVYPPSSGED CCCCCCCCCCCCCCC	16.04	26552605
188	Phosphorylation	PSSVYPPSSGEDYGR CCCCCCCCCCCCCCC	46.61	25159151
189	Phosphorylation	SSVYPPSSGEDYGRD CCCCCCCCCCCCCCC	52.56	28985074
193	Phosphorylation	PPSSGEDYGRDATAY CCCCCCCCCCCCCCC	15.12	26552605
198	Phosphorylation	EDYGRDATAYPSAKT CCCCCCCCCCCCCCC	30.89	26074081
200	Phosphorylation	YGRDATAYPSAKTPS CCCCCCCCCCCCCCC	8.05	26074081
202	Phosphorylation	RDATAYPSAKTPSST CCCCCCCCCCCCCCC	29.71	26074081
205	Phosphorylation	TAYPSAKTPSSTYPA CCCCCCCCCCCCCCC	28.28	26074081
207	Phosphorylation	YPSAKTPSSTYPAPF CCCCCCCCCCCCCCE	40.31	26074081
208	Phosphorylation	PSAKTPSSTYPAPFY CCCCCCCCCCCCCEE	32.91	26074081
209	Phosphorylation	SAKTPSSTYPAPFYV CCCCCCCCCCCCEEE	37.55	26074081
210	Phosphorylation	AKTPSSTYPAPFYVA CCCCCCCCCCCEEEE	10.19	26074081
229	Phosphorylation	HPSAELWSPPGQAGF CCCCHHCCCCCCCCC	33.56	26074081
244	Phosphorylation	GPMLGGGSSPLPLPP CCCCCCCCCCCCCCC	31.86	26074081
245	Phosphorylation	PMLGGGSSPLPLPPG CCCCCCCCCCCCCCC	33.46	28464451
253	Phosphorylation	PLPLPPGSGPVGSSG CCCCCCCCCCCCCCC	45.77	26074081
292	Phosphorylation	GGLPSASSFSSAPGA CCCCCHHHHCCCCCC	28.94	20068231
294	Phosphorylation	LPSASSFSSAPGATY CCCHHHHCCCCCCCC	27.77	23898821
295	Phosphorylation	PSASSFSSAPGATYG CCHHHHCCCCCCCCC	36.15	23898821
300	Phosphorylation	FSSAPGATYGGVSSH HCCCCCCCCCCCCCC	28.72	20068231
301	Phosphorylation	SSAPGATYGGVSSHT CCCCCCCCCCCCCCC	16.02	23898821
305	Phosphorylation	GATYGGVSSHTPPVS CCCCCCCCCCCCCCC	21.48	26074081
306	Phosphorylation	ATYGGVSSHTPPVSG CCCCCCCCCCCCCCC	29.04	20068231
308	O-linked_Glycosylation	YGGVSSHTPPVSGAD CCCCCCCCCCCCCCC	31.10	OGP
308	Phosphorylation	YGGVSSHTPPVSGAD CCCCCCCCCCCCCCC	31.10	20068231
312	Phosphorylation	SSHTPPVSGADSLLG CCCCCCCCCCCCCCC	33.75	23898821
316	Phosphorylation	PPVSGADSLLGSRGT CCCCCCCCCCCCCCC	25.59	23898821
320	Phosphorylation	GADSLLGSRGTTAGS CCCCCCCCCCCCCCC	27.75	23898821
327	Phosphorylation	SRGTTAGSSGDALGK CCCCCCCCCHHHHHH	28.78	28634120
328	Phosphorylation	RGTTAGSSGDALGKA CCCCCCCCHHHHHHH	39.51	21815630
334	Acetylation	SSGDALGKALASIYS CCHHHHHHHHHHHHC	40.87	22207202
338	Phosphorylation	ALGKALASIYSPDHS HHHHHHHHHHCCCCC	23.94	28464451
340	Phosphorylation	GKALASIYSPDHSSN HHHHHHHHCCCCCCC	16.20	30576142
341	Phosphorylation	KALASIYSPDHSSNN HHHHHHHCCCCCCCC	23.37	23927012
345	Phosphorylation	SIYSPDHSSNNFSSS HHHCCCCCCCCCCCC	41.99	28464451
346	Phosphorylation	IYSPDHSSNNFSSSP HHCCCCCCCCCCCCC	32.16	28464451
350	Phosphorylation	DHSSNNFSSSPSTPV CCCCCCCCCCCCCCC	31.84	23927012
351	Phosphorylation	HSSNNFSSSPSTPVG CCCCCCCCCCCCCCC	41.97	23927012
352	Phosphorylation	SSNNFSSSPSTPVGS CCCCCCCCCCCCCCC	22.98	23927012
354	Phosphorylation	NNFSSSPSTPVGSPQ CCCCCCCCCCCCCCC	47.49	23927012
355	Phosphorylation	NFSSSPSTPVGSPQG CCCCCCCCCCCCCCC	25.94	23927012
359	Phosphorylation	SPSTPVGSPQGLAGT CCCCCCCCCCCCCCC	17.81	23927012
366	Phosphorylation	SPQGLAGTSQWPRAG CCCCCCCCCCCCCCC	16.49	28450419
367	Phosphorylation	PQGLAGTSQWPRAGA CCCCCCCCCCCCCCC	29.36	28450419
371	Methylation	AGTSQWPRAGAPGAL CCCCCCCCCCCCCCC	42.57	-
379	Phosphorylation	AGAPGALSPSYDGGL CCCCCCCCCCCCCCC	15.97	22167270
379 (in isoform 2)	Phosphorylation	-	15.97	18669648
381	Phosphorylation	APGALSPSYDGGLHG CCCCCCCCCCCCCCH	32.26	22167270
381 (in isoform 2)	Phosphorylation	-	32.26	18669648
382	Phosphorylation	PGALSPSYDGGLHGL CCCCCCCCCCCCCHH	23.22	23927012
382 (in isoform 2)	Phosphorylation	-	23.22	18669648
391	Phosphorylation	GGLHGLQSKIEDHLD CCCCHHHHHHHHHHH	40.41	23927012
392	Sumoylation	GLHGLQSKIEDHLDE CCCHHHHHHHHHHHH	36.83	-
411	Phosphorylation	LRSHAVGTAGDMHTL HHHCCCCCCCCHHHC	22.37	-
434	Phosphorylation	SGFTGPMSLGGRHAG CCCCCCCCCCCCCCC	27.31	28555341
463 (in isoform 3)	Phosphorylation	-	18.93	25159151
491	Phosphorylation	GLGRAGATAAASEIK CCCHHHHHHHHHHHH	18.86	27174698
495	Phosphorylation	AGATAAASEIKREEK HHHHHHHHHHHHHHH	34.82	27174698
498	Sumoylation	TAAASEIKREEKEDE HHHHHHHHHHHHHCC	50.10	-
498	Sumoylation	TAAASEIKREEKEDE HHHHHHHHHHHHHCC	50.10	28112733
502	Sumoylation	SEIKREEKEDEENTS HHHHHHHHHCCCCCC	66.76	-
508	Phosphorylation	EKEDEENTSAADHSE HHHCCCCCCCCCCCH	24.03	29978859
509	Phosphorylation	KEDEENTSAADHSEE HHCCCCCCCCCCCHH	32.80	29255136
514	Phosphorylation	NTSAADHSEEEKKEL CCCCCCCCHHHHHHH	47.45	23401153
528	Phosphorylation	LKAPRARTSPDEDED HHCCCCCCCCCCCCC	43.56	30576142
528 (in isoform 2)	Phosphorylation	-	43.56	27273156
529	Phosphorylation	KAPRARTSPDEDEDD HCCCCCCCCCCCCCC	25.46	25218447
529 (in isoform 2)	Phosphorylation	-	25.46	23927012
530 (in isoform 2)	Phosphorylation	-	48.69	23927012
531 (in isoform 2)	Phosphorylation	-	75.61	27273156
536 (in isoform 2)	Phosphorylation	-	48.32	30108239
570	Ubiquitination	RDINEAFKELGRMCQ HHHHHHHHHHHHHHH	60.11	-
579 (in isoform 2)	Phosphorylation	-	9.33	-
584	Ubiquitination	QLHLNSEKPQTKLLI HHHCCCCCCCCEEHH	42.10	-
614	Ubiquitination	RERNLNPKAACLKRR HHCCCCHHHHHHHHH	47.76	-
625	Sumoylation	LKRREEEKVSGVVGD HHHHHHHHHCCCCCC	45.01	28112733
625	Ubiquitination	LKRREEEKVSGVVGD HHHHHHHHHCCCCCC	45.01	-

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
39	S	Phosphorylation	Kinase	PAK5	Q9P286	PSP
48	S	Phosphorylation	Kinase	CDK2	P24941	GPS
48	S	Phosphorylation	Kinase	CDK4	P11802	GPS
139	S	Phosphorylation	Kinase	CDK2	P24941	PSP
139	S	Phosphorylation	Kinase	CDK4	P11802	PSP
154	S	Phosphorylation	Kinase	CDK2	P24941	GPS
154	S	Phosphorylation	Kinase	CDK4	P11802	GPS
245	S	Phosphorylation	Kinase	CDK4	P11802	PSP
245	S	Phosphorylation	Kinase	CDK2	P24941	PSP
341	S	Phosphorylation	Kinase	MAP3K10	Q02779	GPS
352	S	Phosphorylation	Kinase	MAP3K10	Q02779	GPS
352	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
355	T	Phosphorylation	Kinase	MAP3K10	Q02779	GPS
355	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
355	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
355	T	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
359	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
359	S	Phosphorylation	Kinase	MAP3K10	Q02779	GPS
379	S	Phosphorylation	Kinase	MAP3K10	Q02779	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFE2_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 TFE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HAND2_HUMAN	HAND2	physical	11812799
ID3_HUMAN	ID3	physical	9525934
TFE2_HUMAN	TCF3	physical	12435739
EP300_HUMAN	EP300	physical	12435739
CBP_HUMAN	CREBBP	physical	12435739
KAT2B_HUMAN	KAT2B	physical	12435739
KAT2B_HUMAN	KAT2B	genetic	12435739
EP300_HUMAN	EP300	genetic	12435739
CBP_HUMAN	CREBBP	genetic	12435739
TAL1_HUMAN	TAL1	physical	16407974
LDB1_HUMAN	LDB1	physical	16407974
MTG16_HUMAN	CBFA2T3	physical	16407974
ELK3_HUMAN	ELK3	physical	8918463
MYOD1_HUMAN	MYOD1	physical	9242638
MYF5_HUMAN	MYF5	physical	9242638
MYF6_HUMAN	MYF6	physical	9242638
MYOG_HUMAN	MYOG	physical	9242638
TWST1_HUMAN	TWIST1	physical	10749989
DAXX_HUMAN	DAXX	physical	19308989
ID1_HUMAN	ID1	physical	19125693
VDR_HUMAN	VDR	physical	17250953
HDAC2_HUMAN	HDAC2	physical	17250953
DNMT1_HUMAN	DNMT1	physical	17250953
RB_HUMAN	RB1	physical	10866689
TFE2_HUMAN	TCF3	physical	22354994
ID4_HUMAN	ID4	physical	22354994
ID1_HUMAN	ID1	physical	22354994
ID2_HUMAN	ID2	physical	22354994
KDM1A_HUMAN	KDM1A	physical	22354994
ANM5_HUMAN	PRMT5	physical	22354994
RM37_HUMAN	MRPL37	physical	22354994
RL23A_HUMAN	RPL23A	physical	22354994
QCR2_HUMAN	UQCRC2	physical	22354994
RM49_HUMAN	MRPL49	physical	22354994
TWST1_HUMAN	TWIST1	physical	22354994
DDX17_HUMAN	DDX17	physical	22354994
SAFB1_HUMAN	SAFB	physical	22354994
IF5A1_HUMAN	EIF5A	physical	22354994
MYO1B_HUMAN	MYO1B	physical	22354994
ELAV1_HUMAN	ELAVL1	physical	22354994
ID3_HUMAN	ID3	physical	22354994
GSE1_HUMAN	GSE1	physical	22354994
DIC_HUMAN	SLC25A10	physical	22354994
BHA15_HUMAN	BHLHA15	physical	22354994
PIP_HUMAN	PIP	physical	22354994
P5CS_HUMAN	ALDH18A1	physical	22354994
SF3A3_HUMAN	SF3A3	physical	22354994
DJC10_HUMAN	DNAJC10	physical	22354994
RL36A_HUMAN	RPL36A	physical	22354994
MIC60_HUMAN	IMMT	physical	22354994
RS13_HUMAN	RPS13	physical	22354994
DDX20_HUMAN	DDX20	physical	22354994
TET2_HUMAN	TET2	physical	22354994
PRP8_HUMAN	PRPF8	physical	22354994
RCOR1_HUMAN	RCOR1	physical	22354994
TCF24_HUMAN	TCF24	physical	22354994
RL14_HUMAN	RPL14	physical	22354994
PON2_HUMAN	PON2	physical	22354994
SSBP_HUMAN	SSBP1	physical	22354994
RL31_HUMAN	RPL31	physical	22354994
RM44_HUMAN	MRPL44	physical	22354994
CN166_HUMAN	C14orf166	physical	22354994
SPIN1_HUMAN	SPIN1	physical	22354994
TCPB_HUMAN	CCT2	physical	22354994
MYL6B_HUMAN	MYL6B	physical	22354994
MIC19_HUMAN	CHCHD3	physical	22354994
AT2A3_HUMAN	ATP2A3	physical	22354994
LANC2_HUMAN	LANCL2	physical	22354994
NHRF1_HUMAN	SLC9A3R1	physical	22354994
TIM50_HUMAN	TIMM50	physical	22354994
ERLN2_HUMAN	ERLIN2	physical	22354994
RM39_HUMAN	MRPL39	physical	22354994
ATOH8_HUMAN	ATOH8	physical	22354994
SERPH_HUMAN	SERPINH1	physical	22354994
SETLP_HUMAN	SETSIP	physical	22354994
SON_HUMAN	SON	physical	22354994
FBRL_HUMAN	FBL	physical	22354994
ADT1_HUMAN	SLC25A4	physical	22354994
EF1A2_HUMAN	EEF1A2	physical	22354994
LEG7_HUMAN	LGALS7	physical	22354994
C1QBP_HUMAN	C1QBP	physical	22354994
CBPD_HUMAN	CPD	physical	22354994
RM23_HUMAN	MRPL23	physical	22354994
HEN2_HUMAN	NHLH2	physical	22354994
RL13_HUMAN	RPL13	physical	22354994
CX7A2_HUMAN	COX7A2	physical	22354994
CYTA_HUMAN	CSTA	physical	22354994
PCBP1_HUMAN	PCBP1	physical	22354994
NDUB4_HUMAN	NDUFB4	physical	22354994
TFF3_HUMAN	TFF3	physical	22354994
FILA2_HUMAN	FLG2	physical	22354994
HNRPR_HUMAN	HNRNPR	physical	22354994
ERAL1_HUMAN	ERAL1	physical	22354994
RPN2_HUMAN	RPN2	physical	22354994
RBM39_HUMAN	RBM39	physical	22354994
RL24_HUMAN	RPL24	physical	22354994
LBR_HUMAN	LBR	physical	22354994
CASPE_HUMAN	CASP14	physical	22354994
STK38_HUMAN	STK38	physical	22354994
CALX_HUMAN	CANX	physical	22354994
UBC9_RAT	Ube2i	physical	9013644
TLE1_HUMAN	TLE1	physical	18611861
KAT2A_HUMAN	KAT2A	physical	23044487
TRRAP_HUMAN	TRRAP	physical	23044487
SUPT3_HUMAN	SUPT3H	physical	23044487
TAD2A_HUMAN	TADA2A	physical	23044487
TFE2_HUMAN	TCF3	physical	9050988
MYOD1_HUMAN	MYOD1	physical	9050988
MYOD1_MOUSE	Myod1	physical	9050988
HTF4_MOUSE	Tcf12	physical	9050988
SCX_MOUSE	Scx	physical	9050988
TWST2_MOUSE	Twist2	physical	9050988
USF1_MOUSE	Usf1	physical	9050988
RFA1_MOUSE	Rpa1	physical	9050988
NUCL_MOUSE	Ncl	physical	9050988
USF1_HUMAN	USF1	physical	9050988
SCX_HUMAN	SCX	physical	9050988
TCF21_HUMAN	TCF21	physical	21771727
MAPK3_HUMAN	MAPKAPK3	physical	10781029
MAPK2_HUMAN	MAPKAPK2	physical	10781029
TCAF1_HUMAN	FAM115A	physical	25416956
CBP_HUMAN	CREBBP	physical	15507449
KAT2B_HUMAN	KAT2B	physical	15507449
CBP_HUMAN	CREBBP	physical	22387215
CBP_HUMAN	CREBBP	physical	22207202
NDF1_HUMAN	NEUROD1	physical	14752053
EP300_HUMAN	EP300	physical	14752053
ID3_HUMAN	ID3	physical	9242638
ID2_HUMAN	ID2	physical	9242638
ID1_HUMAN	ID1	physical	9242638
BHE40_MOUSE	Bhlhe40	physical	9050988
BHE40_HUMAN	BHLHE40	physical	9050988
PARP1_HUMAN	PARP1	physical	9050988
TCF15_MOUSE	Tcf15	physical	9050988
TFE2_MOUSE	Tcf3	physical	9050988
PSMD4_HUMAN	PSMD4	physical	9235903

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 TFE2_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-139 AND SER-359, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASSSPECTROMETRY.	19369195 [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-379, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT THR-531 (ISOFORM 2), AND MASS SPECTROMETRY.	18669648 [Abstract]