dbPTM

TFDP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFDP1_HUMAN
UniProt AC	Q14186
Protein Name	Transcription factor Dp-1
Gene Name	TFDP1
Organism	Homo sapiens (Human).
Sequence Length	410
Subcellular Localization	Nucleus . Cytoplasm . Shuttles between the cytoplasm and nucleus and translocates into the nuclear compartment upon heterodimerization with E2F1.
Protein Description	Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. [PubMed: 8405995]
Protein Sequence	MAKDAGLIEANGELKVFIDQNLSPGKGVVSLVAVHPSTVNPLGKQLLPKTFGQSNVNIAQQVVIGTPQRPAASNTLVVGSPHTPSTHFASQNQPSDSSPWSAGKRNRKGEKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVAEFSAADNHILPNESAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEVERQRRLERIKQKQSQLQELILQQIAFKNLVQRNRHAEQQASRPPPPNSVIHLPFIIVNTSKKTVIDCSISNDKFEYLFNFDNTFEIHDDIEVLKRMGMACGLESGSCSAEDLKMARSLVPKALEPYVTEMAQGTVGGVFITTAGSTSNGTRFSASDLTNGADGMLATSSNGSQYSGSRVETPVSYVGEDDEEDDDFNENDEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKDAGLIEA -----CCCCCCEEEE	46.98	19608861
3	Ubiquitination	-----MAKDAGLIEA -----CCCCCCEEEE	46.98	19608861
23	Phosphorylation	VFIDQNLSPGKGVVS EEEECCCCCCCCEEE	38.87	19664994
26	Ubiquitination	DQNLSPGKGVVSLVA ECCCCCCCCEEEEEE	52.49	-
27	Ubiquitination	QNLSPGKGVVSLVAV CCCCCCCCEEEEEEE	30.86	-
30	Phosphorylation	SPGKGVVSLVAVHPS CCCCCEEEEEEECHH	18.08	28464451
37	Phosphorylation	SLVAVHPSTVNPLGK EEEEECHHHCCCCCH	30.06	24732914
38	Phosphorylation	LVAVHPSTVNPLGKQ EEEECHHHCCCCCHH	28.84	24732914
44	Ubiquitination	STVNPLGKQLLPKTF HHCCCCCHHHCCCCC	45.51	21890473
44	Acetylation	STVNPLGKQLLPKTF HHCCCCCHHHCCCCC	45.51	26051181
44	Ubiquitination	STVNPLGKQLLPKTF HHCCCCCHHHCCCCC	45.51	21890473
73	Phosphorylation	TPQRPAASNTLVVGS CCCCCCCCCEEEECC	32.24	20873877
75	Phosphorylation	QRPAASNTLVVGSPH CCCCCCCEEEECCCC	20.59	28985074
80	Phosphorylation	SNTLVVGSPHTPSTH CCEEEECCCCCCCCC	11.25	20873877
83	Phosphorylation	LVVGSPHTPSTHFAS EEECCCCCCCCCCCC	23.48	28985074
85	Phosphorylation	VGSPHTPSTHFASQN ECCCCCCCCCCCCCC	35.35	20873877
86	Phosphorylation	GSPHTPSTHFASQNQ CCCCCCCCCCCCCCC	23.40	20873877
90	Phosphorylation	TPSTHFASQNQPSDS CCCCCCCCCCCCCCC	28.81	20873877
91	Ubiquitination	PSTHFASQNQPSDSS CCCCCCCCCCCCCCC	49.50	-
92	Ubiquitination	STHFASQNQPSDSSP CCCCCCCCCCCCCCC	53.92	-
95	Phosphorylation	FASQNQPSDSSPWSA CCCCCCCCCCCCCCC	40.12	20873877
95	Ubiquitination	FASQNQPSDSSPWSA CCCCCCCCCCCCCCC	40.12	-
97	Phosphorylation	SQNQPSDSSPWSAGK CCCCCCCCCCCCCCC	42.51	20873877
98	Phosphorylation	QNQPSDSSPWSAGKR CCCCCCCCCCCCCCC	35.06	20873877
101	Phosphorylation	PSDSSPWSAGKRNRK CCCCCCCCCCCCCCC	30.44	20873877
104	Acetylation	SSPWSAGKRNRKGEK CCCCCCCCCCCCCCC	46.33	26051181
120	Phosphorylation	GKGLRHFSMKVCEKV CCCHHHHHHHHHHHH	16.15	24719451
122	Ubiquitination	GLRHFSMKVCEKVQR CHHHHHHHHHHHHHH	42.40	-
122	Ubiquitination	GLRHFSMKVCEKVQR CHHHHHHHHHHHHHH	42.40	-
124	Ubiquitination	RHFSMKVCEKVQRKG HHHHHHHHHHHHHHC	3.32	-
126	Acetylation	FSMKVCEKVQRKGTT HHHHHHHHHHHHCCC	38.24	25953088
126	Ubiquitination	FSMKVCEKVQRKGTT HHHHHHHHHHHHCCC	38.24	-
130	Ubiquitination	VCEKVQRKGTTSYNE HHHHHHHHCCCCHHH	43.44	-
132	Phosphorylation	EKVQRKGTTSYNEVA HHHHHHCCCCHHHHH	18.66	26552605
133	Phosphorylation	KVQRKGTTSYNEVAD HHHHHCCCCHHHHHH	37.57	26552605
134	Phosphorylation	VQRKGTTSYNEVADE HHHHCCCCHHHHHHH	26.29	26552605
135	Phosphorylation	QRKGTTSYNEVADEL HHHCCCCHHHHHHHH	17.16	26552605
139	Ubiquitination	TTSYNEVADELVAEF CCCHHHHHHHHHHHH	9.81	-
147	Phosphorylation	DELVAEFSAADNHIL HHHHHHHHHHCCCCC	17.66	26552605
158	Phosphorylation	NHILPNESAYDQKNI CCCCCCCCCCCCHHH	38.48	26552605
160	Phosphorylation	ILPNESAYDQKNIRR CCCCCCCCCCHHHHH	28.34	26552605
163	Ubiquitination	NESAYDQKNIRRRVY CCCCCCCHHHHHHHH	51.98	-
170	Phosphorylation	KNIRRRVYDALNVLM HHHHHHHHHHHHHHH	8.16	25072903
180	N-linked_Glycosylation	LNVLMAMNIISKEKK HHHHHHHHHHCCCCC	20.92	-
180	N-linked_Glycosylation	LNVLMAMNIISKEKK HHHHHHHHHHCCCCC	20.92	19349973
183	Phosphorylation	LMAMNIISKEKKEIK HHHHHHHCCCCCCCE	30.85	22817900
190	Ubiquitination	SKEKKEIKWIGLPTN CCCCCCCEEEECCCC	33.57	-
217	Ubiquitination	QRRLERIKQKQSQLQ HHHHHHHHHHHHHHH	58.63	-
219	Ubiquitination	RLERIKQKQSQLQEL HHHHHHHHHHHHHHH	47.09	-
221	Phosphorylation	ERIKQKQSQLQELIL HHHHHHHHHHHHHHH	39.63	-
225	Ubiquitination	QKQSQLQELILQQIA HHHHHHHHHHHHHHH	46.50	-
234	Ubiquitination	ILQQIAFKNLVQRNR HHHHHHHHHHHHHHH	40.11	-
248	Phosphorylation	RHAEQQASRPPPPNS HHHHHHHCCCCCCCC	40.77	28787133
301	Acetylation	HDDIEVLKRMGMACG CCHHHHHHHCCCCCC	45.58	7683649
311	Phosphorylation	GMACGLESGSCSAED CCCCCCCCCCCCHHH	40.84	27732954
313	Phosphorylation	ACGLESGSCSAEDLK CCCCCCCCCCHHHHH	17.74	27732954
315	Phosphorylation	GLESGSCSAEDLKMA CCCCCCCCHHHHHHH	36.07	27732954
320	Ubiquitination	SCSAEDLKMARSLVP CCCHHHHHHHHHHCH	42.72	21890473
360	Phosphorylation	TSNGTRFSASDLTNG CCCCCEECHHHCCCC	24.46	27251275
362	Phosphorylation	NGTRFSASDLTNGAD CCCEECHHHCCCCCC	31.77	27251275
365	Phosphorylation	RFSASDLTNGADGML EECHHHCCCCCCCCE	36.27	27251275
374	Phosphorylation	GADGMLATSSNGSQY CCCCCEEECCCCCCC	28.82	27251275
375	Phosphorylation	ADGMLATSSNGSQYS CCCCEEECCCCCCCC	19.05	26714015
376	Phosphorylation	DGMLATSSNGSQYSG CCCEEECCCCCCCCC	40.64	27251275
379	Phosphorylation	LATSSNGSQYSGSRV EEECCCCCCCCCCCE	30.14	27251275
381	Phosphorylation	TSSNGSQYSGSRVET ECCCCCCCCCCCEEC	19.39	27251275
382	Phosphorylation	SSNGSQYSGSRVETP CCCCCCCCCCCEECC	23.74	27251275
384	Phosphorylation	NGSQYSGSRVETPVS CCCCCCCCCEECCCE	27.49	27251275
388	Phosphorylation	YSGSRVETPVSYVGE CCCCCEECCCEECCC	26.57	28985074
391	Phosphorylation	SRVETPVSYVGEDDE CCEECCCEECCCCCC	18.46	28985074
392	Phosphorylation	RVETPVSYVGEDDEE CEECCCEECCCCCCC	16.83	27732954

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
23	S	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFDP1_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 TFDP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TP53B_HUMAN	TP53BP1	physical	8896460
CDK3_HUMAN	CDK3	physical	8846921
E2F1_HUMAN	E2F1	physical	7892279
E2F4_HUMAN	E2F4	physical	7892279
E2F5_HUMAN	E2F5	physical	7892279
E2F1_HUMAN	E2F1	physical	22629304
E2F1_HUMAN	E2F1	physical	9199321
E2F4_HUMAN	E2F4	physical	9199321
E2F1_HUMAN	E2F1	physical	8816798
E2F6_HUMAN	E2F6	physical	9704927
E2F1_HUMAN	E2F1	physical	9704927
E2F1_HUMAN	E2F1	physical	8832394
E2F2_HUMAN	E2F2	physical	8832394
E2F3_HUMAN	E2F3	physical	8832394
CBP_HUMAN	CREBBP	physical	8932363
E2F1_HUMAN	E2F1	physical	15133492

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 TFDP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-23, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	19413330 [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-23, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	19007248 [Abstract]