E2F2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: E2F2_HUMAN
• UniProt AC: Q14209
• Protein Name: Transcription factor E2F2
• Gene Name: E2F2
• Organism: Homo sapiens (Human).
• Sequence Length: 437
• 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. E2F2 binds specifically to RB1 in a cell-cycle dependent manner..
• Protein Sequence: MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPSTSTLCPSPDSAQPSSSTDPSIMEPTASSVPAPAPTPQQAPPPPSLVPLEATDSLLELPHPLLQQTEDQFLSPTLACSSPLISFSPSLDQDDYLWGLEAGEGISDLFDSYDLGDLLIN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	QGPRALASAAGQTPK CCHHHHHHHCCCCCC	21.36	22210691
15	Phosphorylation	LASAAGQTPKVVPAM HHHHCCCCCCCCCCC	24.94	29414761
88	Ubiquitination	GRLPAKRKLDLEGIG CCCCCCCCCCCCCCC	45.72	-
104	Phosphorylation	PVVPEFPTPKGKCIR CCCCCCCCCCCCEEE	42.84	24719451
117	Phosphorylation	IRVDGLPSPKTPKSP EEECCCCCCCCCCCC	44.03	30266825
119	Acetylation	VDGLPSPKTPKSPGE ECCCCCCCCCCCCCC	80.12	60539
119	Ubiquitination	VDGLPSPKTPKSPGE ECCCCCCCCCCCCCC	80.12	29967540
120	Phosphorylation	DGLPSPKTPKSPGEK CCCCCCCCCCCCCCC	39.06	-
122	Acetylation	LPSPKTPKSPGEKTR CCCCCCCCCCCCCCC	74.62	60543
123	Phosphorylation	PSPKTPKSPGEKTRY CCCCCCCCCCCCCCC	39.06	24719451
127	Acetylation	TPKSPGEKTRYDTSL CCCCCCCCCCCCCHH	44.19	60547
130	Phosphorylation	SPGEKTRYDTSLGLL CCCCCCCCCCHHHHH	28.89	30576142
132	Phosphorylation	GEKTRYDTSLGLLTK CCCCCCCCHHHHHHH	19.54	30576142
133	Phosphorylation	EKTRYDTSLGLLTKK CCCCCCCHHHHHHHH	19.97	30576142
139	Ubiquitination	TSLGLLTKKFIYLLS CHHHHHHHHHHHHHH	45.73	29967540
187	Ubiquitination	QLIRKKAKNNIQWVG HHHHHHHHHCCCEEC	60.45	-
206	Ubiquitination	EDPTRPGKQQQLGQE CCCCCCCHHHHHHHH	47.84	29967540
234	Phosphorylation	LIQSCSLSFKHLTED HHHHHCCCCCCCCCC	18.89	24719451
236	Ubiquitination	QSCSLSFKHLTEDKA HHHCCCCCCCCCCCC	34.04	29967540
245	Acetylation	LTEDKANKRLAYVTY CCCCCCCCEEEEEEH	54.36	19829883
262	Ubiquitination	IRAVGNFKEQTVIAV HHHHCCCCCCEEEEE	53.57	-
270	Ubiquitination	EQTVIAVKAPPQTRL CCEEEEEECCCCCEE	46.27	29967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of E2F2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of E2F2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of E2F2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPIB_HUMAN	SPIB	physical	12748276
RYBP_HUMAN	RYBP	physical	12411495
KMT5A_HUMAN	SETD8	physical	12411495
R144A_HUMAN	RNF144A	physical	12411495
FHL2_HUMAN	FHL2	physical	12411495
RB_HUMAN	RB1	physical	12502741
SP1_MOUSE	Sp1	physical	8657141
KMT2A_HUMAN	KMT2A	physical	16951254
KMT2D_HUMAN	KMT2D	physical	16951254
ATAD2_HUMAN	ATAD2	physical	20855524
RB_HUMAN	RB1	physical	17380128
RB_HUMAN	RB1	physical	8246996
GIT2_HUMAN	GIT2	physical	21988832
GNB5_HUMAN	GNB5	physical	21988832
E2F1_HUMAN	E2F1	physical	25241761
UCHL5_HUMAN	UCHL5	physical	26396186

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.