dbPTM

E2F4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	E2F4_HUMAN
UniProt AC	Q16254
Protein Name	Transcription factor E2F4
Gene Name	E2F4
Organism	Homo sapiens (Human).
Sequence Length	413
Subcellular Localization	Nucleus.
Protein Description	Transcription activator that binds DNA cooperatively with DP proteins 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. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis..
Protein Sequence	MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSVSGPIEVLLVNKEAWSSPPVAVPVPPPEDLLQSPSAVSTPPPLPKPALAQSQEASRPNSPQLTPTAVPGSAEVQGMAGPAAEITVSGGPGTDSKDSGELSSLPLGPTTLDTRPLQSSALLDSSSSSSSSSSSSSNSNSSSSSGPNPSTSFEPIKADPTGVLELPKELSEIFDPTRECMSSELLEELMSSEVFAPLLRLSPPPGDHDYIYNLDESEGVCDLFDVPVLNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEAGPQAP ------CCCCCCCCC	18.49	19413330
14	Phosphorylation	QAPPPPGTPSRHEKS CCCCCCCCCCHHHHH	24.70	23401153
16	Phosphorylation	PPPPGTPSRHEKSLG CCCCCCCCHHHHHHH	46.22	29255136
20	Ubiquitination	GTPSRHEKSLGLLTT CCCCHHHHHHHHHHH	44.87	29967540
21	Phosphorylation	TPSRHEKSLGLLTTK CCCHHHHHHHHHHHH	25.37	26074081
28	Ubiquitination	SLGLLTTKFVSLLQE HHHHHHHHHHHHHHH	38.23	-
37	Ubiquitination	VSLLQEAKDGVLDLK HHHHHHHHHCCHHHH	55.02	22817900
44	Ubiquitination	KDGVLDLKLAADTLA HHCCHHHHHHHHHHH	35.43	29967540
59	Phosphorylation	VRQKRRIYDITNVLE HHHHHHHHHHHHHHH	10.24	-
73	Ubiquitination	EGIGLIEKKSKNSIQ HHHCCEEECCCCCCC	56.18	-
74	Ubiquitination	GIGLIEKKSKNSIQW HHCCEEECCCCCCCC	54.60	-
82	Ubiquitination	SKNSIQWKGVGPGCN CCCCCCCCCCCCCCC	27.61	29967540
96	Acetylation	NTREIADKLIELKAE CHHHHHHHHHHHHHH	42.20	7709705
96	Ubiquitination	NTREIADKLIELKAE CHHHHHHHHHHHHHH	42.20	29967540
101	Ubiquitination	ADKLIELKAEIEELQ HHHHHHHHHHHHHHH	31.05	29967540
139	Phosphorylation	VQNSCLAYVTHEDIC HHHCHHEECCHHHHH	7.91	-
141	Phosphorylation	NSCLAYVTHEDICRC HCHHEECCHHHHHHH	13.58	-
201	Phosphorylation	LVNKEAWSSPPVAVP EEECCCCCCCCEECC	39.76	28102081
202	Phosphorylation	VNKEAWSSPPVAVPV EECCCCCCCCEECCC	23.63	28102081
218	Phosphorylation	PPEDLLQSPSAVSTP CHHHHHCCCCCCCCC	22.31	26657352
220	Phosphorylation	EDLLQSPSAVSTPPP HHHHCCCCCCCCCCC	46.69	22199227
223	Phosphorylation	LQSPSAVSTPPPLPK HCCCCCCCCCCCCCC	34.61	22199227
224	Phosphorylation	QSPSAVSTPPPLPKP CCCCCCCCCCCCCCH	32.96	26657352
236	Phosphorylation	PKPALAQSQEASRPN CCHHHHCCCCCCCCC	25.12	26074081
240	Phosphorylation	LAQSQEASRPNSPQL HHCCCCCCCCCCCCC	47.74	30576142
244	Phosphorylation	QEASRPNSPQLTPTA CCCCCCCCCCCCCCC	19.39	30576142
248	Phosphorylation	RPNSPQLTPTAVPGS CCCCCCCCCCCCCCC	17.22	26074081
250	Phosphorylation	NSPQLTPTAVPGSAE CCCCCCCCCCCCCEE	34.74	25002506
255	Phosphorylation	TPTAVPGSAEVQGMA CCCCCCCCEEECCCC	18.39	25002506
269	Phosphorylation	AGPAAEITVSGGPGT CCCCEEEEEECCCCC	10.50	25002506
271	Phosphorylation	PAAEITVSGGPGTDS CCEEEEEECCCCCCC	29.40	25002506
276	Phosphorylation	TVSGGPGTDSKDSGE EEECCCCCCCCCCCC	39.99	25002506
278	Phosphorylation	SGGPGTDSKDSGELS ECCCCCCCCCCCCCC	37.89	25002506
309	Phosphorylation	SALLDSSSSSSSSSS CCCCCCCCCCCCCCC	37.89	-
310	Phosphorylation	ALLDSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
311	Phosphorylation	LLDSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
312	Phosphorylation	LDSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
313	Phosphorylation	DSSSSSSSSSSSSSN CCCCCCCCCCCCCCC	35.87	-
353	Phosphorylation	LELPKELSEIFDPTR EECCHHHHHHCCCCC	29.73	23917254
359	Phosphorylation	LSEIFDPTRECMSSE HHHHCCCCCHHCCHH	40.73	23186163
373	Phosphorylation	ELLEELMSSEVFAPL HHHHHHHCCCCCHHH	35.65	26074081
374	Phosphorylation	LLEELMSSEVFAPLL HHHHHHCCCCCHHHH	24.66	26074081
384	Phosphorylation	FAPLLRLSPPPGDHD CHHHHHCCCCCCCCC	29.00	23663014
392	Phosphorylation	PPPGDHDYIYNLDES CCCCCCCCEEECCCC	11.24	26074081
394	Phosphorylation	PGDHDYIYNLDESEG CCCCCCEEECCCCCC	11.93	23663014
399	Phosphorylation	YIYNLDESEGVCDLF CEEECCCCCCCCCCC	39.04	26074081

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
244	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
384	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of E2F4_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 E2F4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MGAP_HUMAN	MGA	physical	12748276
SPIB_HUMAN	SPIB	physical	12748276
HDAC1_HUMAN	HDAC1	physical	9724731
RBL1_HUMAN	RBL1	physical	12150994
SMAD3_HUMAN	SMAD3	physical	12150994
R144A_HUMAN	RNF144A	physical	12411495
FHL2_HUMAN	FHL2	physical	12411495
RYBP_HUMAN	RYBP	physical	12411495
NECD_MOUSE	Ndn	physical	12198120
TFDP2_HUMAN	TFDP2	physical	10090723
ID3_HUMAN	ID3	physical	20211142
KMT2A_HUMAN	KMT2A	physical	16951254
ID2_HUMAN	ID2	physical	16776654
TRRAP_HUMAN	TRRAP	physical	11418595
KAT2A_HUMAN	KAT2A	physical	11418595
RBL1_HUMAN	RBL1	physical	9858615
RBL2_HUMAN	RBL2	physical	9858615
RB_HUMAN	RB1	physical	9858615
SIN3A_HUMAN	SIN3A	physical	17612494
ASH2L_HUMAN	ASH2L	physical	17612494
ATAD2_HUMAN	ATAD2	physical	20855524
RBL2_HUMAN	RBL2	physical	17671431
RBL1_HUMAN	RBL1	physical	17671431
ANDR_HUMAN	AR	physical	22508987
NCOR2_HUMAN	NCOR2	physical	22508987
HDAC3_HUMAN	HDAC3	physical	22508987
XPO1_HUMAN	XPO1	physical	12860972
RBL2_HUMAN	RBL2	physical	17159899
RBL1_HUMAN	RBL1	physical	8832394
TIF1B_HUMAN	TRIM28	physical	23060449
TFDP1_HUMAN	TFDP1	physical	7958925
TFDP1_HUMAN	TFDP1	physical	7958924
PCM1_HUMAN	PCM1	physical	21988832
RBL2_HUMAN	RBL2	physical	23108140
PML_HUMAN	PML	physical	22002537
RBL2_HUMAN	RBL2	physical	22002537
TFDP1_HUMAN	TFDP1	physical	9501179
TFDP2_HUMAN	TFDP2	physical	9501179
RBL1_HUMAN	RBL1	physical	9501179
RB_HUMAN	RB1	physical	9501179
CDK4_HUMAN	CDK4	physical	27173435

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 E2F4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]