E2F7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: E2F7_HUMAN
• UniProt AC: Q96AV8
• Protein Name: Transcription factor E2F7
• Gene Name: E2F7
• Organism: Homo sapiens (Human).
• Sequence Length: 911
• Subcellular Localization: Nucleus .
• Protein Description: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation..
• Protein Sequence: MEVNCLTLKDLISPRQPRLDFAVEDGENAQKENIFVDRSRMAPKTPIKNEPIDLSKQKKFTPERNPITPVKFVDRQQAEPWTPTANLKMLISAASPDIRDREKKKGLFRPIENKDDAFTDSLQLDVVGDSAVDEFEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRNLQRLGEEQKYEEQMAYLQQKELDLIDYKFGERKKDGDPDSQEQQLLDFSEPDCPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDAPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSSDEELVDVSASVLPELKRETYGQIQVCAKQKLARHGSFNTVQASERIQRKVNSEPSSPYREEQGSGGYSLEIGSLAAVYRQKIEDNSQGKAFASKRVVPPSSSLDPVAPFPVLSVDPEYCVNPLAHPVFSVAQTDLQAFSMQNGLNGQVDVSLASAASAVESLKPALLAGQPLVYVPSASLFMLYGSLQEGPASGSGSERDDRSSEAPATVELSSAPSAQKRLCEERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRASIPLKDIHVNGQLPAAEEISGKATANSLVSSEWGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPAGLNGFNVLLSGSQTPPTVGPSSGQLPSFSVPCMVLPSPPLGPFPVLYSPAMPGPVSSTLGALPNTGPVNFSLPGLGSIAQLLVGPTAVVNPKSSTLPSADPQLQSQPSLNLSPVMSRSHSVVQQPESPVYVGHPVSVVKLHQSPVPVTPKSIQRTHRETFFKTPGSLGDPVLKRRERNQSRNTSSAQRRLEIPSGGAD

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
13	Phosphorylation	LTLKDLISPRQPRLD EEHHHHCCCCCCCCC	22.71	24719451
31	Ubiquitination	EDGENAQKENIFVDR CCCCCCCCCCEEEEH	50.77	29967540
45	Phosphorylation	RSRMAPKTPIKNEPI HHHCCCCCCCCCCCC	29.23	29255136
48	Sumoylation	MAPKTPIKNEPIDLS CCCCCCCCCCCCCHH	57.36	-
48	Sumoylation	MAPKTPIKNEPIDLS CCCCCCCCCCCCCHH	57.36	-
55	Phosphorylation	KNEPIDLSKQKKFTP CCCCCCHHHCCCCCC	29.32	30576142
58	Trimethylation	PIDLSKQKKFTPERN CCCHHHCCCCCCCCC	54.30	-
58	Methylation	PIDLSKQKKFTPERN CCCHHHCCCCCCCCC	54.30	-
61	Phosphorylation	LSKQKKFTPERNPIT HHHCCCCCCCCCCCC	32.87	30266825
68	Phosphorylation	TPERNPITPVKFVDR CCCCCCCCCCEECCH	24.24	25849741
82	Phosphorylation	RQQAEPWTPTANLKM HHHCCCCCCCHHHHH	22.83	25850435
84	Phosphorylation	QAEPWTPTANLKMLI HCCCCCCCHHHHHHH	22.32	25850435
92	Phosphorylation	ANLKMLISAASPDIR HHHHHHHHHCCCCCC	17.51	30266825
95	Phosphorylation	KMLISAASPDIRDRE HHHHHHCCCCCCHHH	23.87	30266825
153	Ubiquitination	SLGLLCQKFLARYPS HHHHHHHHHHHHCCC	41.15	29967540
160	Phosphorylation	KFLARYPSYPLSTEK HHHHHCCCCCCCCCC	30.37	-
204	Ubiquitination	HLVSRVAKNQYGWHG HHHHHHHHCCCCCCC	41.55	-
217	Ubiquitination	HGRHSLPKTLRNLQR CCCCCHHHHHHHHHH	66.54	29967540
230	Ubiquitination	QRLGEEQKYEEQMAY HHHCHHHHHHHHHHH	58.89	29967540
231	Phosphorylation	RLGEEQKYEEQMAYL HHCHHHHHHHHHHHH	25.13	-
241	Ubiquitination	QMAYLQQKELDLIDY HHHHHHHHHHHHHCC	47.48	29967540
249	Ubiquitination	ELDLIDYKFGERKKD HHHHHCCCCCCCCCC	43.05	29967540
261	Phosphorylation	KKDGDPDSQEQQLLD CCCCCCCHHHHHHHH	40.79	20873877
270	Phosphorylation	EQQLLDFSEPDCPSS HHHHHHCCCCCCCCC	48.13	20873877
301	Phosphorylation	FVMLFLVSKTKIVTL CHHHHHHCCCCEEEH	36.43	-
327	Ubiquitination	QDAPDHSKFKTKVRR CCCCCHHHHHHHHHH	47.67	29967540
384	Phosphorylation	ELVDVSASVLPELKR HHHHHCHHHCHHHHH	19.38	-
410	Phosphorylation	QKLARHGSFNTVQAS HHHHHHCCCCHHHHH	14.81	30266825
413	Phosphorylation	ARHGSFNTVQASERI HHHCCCCHHHHHHHH	16.40	30266825
417	Phosphorylation	SFNTVQASERIQRKV CCCHHHHHHHHHHHH	15.43	20068231
463	Ubiquitination	IEDNSQGKAFASKRV CCCCCCCCCCCCCCC	32.47	29967540
467	O-linked_Glycosylation	SQGKAFASKRVVPPS CCCCCCCCCCCCCCH	17.97	30620550
578	Phosphorylation	SERDDRSSEAPATVE CCCCCCCCCCCCEEE	38.38	-
594	Acetylation	SSAPSAQKRLCEERK CCCCHHHHHHHHHCC	47.24	25953088
623	Phosphorylation	EYEDGPLSLVMPKKP CCCCCCCEEECCCCC	23.27	-
631	Phosphorylation	LVMPKKPSDSTDLAS EECCCCCCCCCCCCC	53.74	30619164
633	Phosphorylation	MPKKPSDSTDLASPK CCCCCCCCCCCCCCC	28.32	30619164
634	Phosphorylation	PKKPSDSTDLASPKT CCCCCCCCCCCCCCC	39.77	30619164
638	Phosphorylation	SDSTDLASPKTMGNR CCCCCCCCCCCCCCC	33.94	20363803
651	Acetylation	NRASIPLKDIHVNGQ CCCCCCHHHCEECCC	49.64	25953088
692	Phosphorylation	NTDVEKPSKENESTK CCCCCCCCCCCCCCC	64.76	-
818	Phosphorylation	SADPQLQSQPSLNLS CCCHHHHCCCCCCCC	53.29	28102081
821	Phosphorylation	PQLQSQPSLNLSPVM HHHHCCCCCCCCCCC	23.42	25850435
825	Phosphorylation	SQPSLNLSPVMSRSH CCCCCCCCCCCCCCC	17.86	25850435
829	Phosphorylation	LNLSPVMSRSHSVVQ CCCCCCCCCCCCCCC	30.75	25850435
831	Phosphorylation	LSPVMSRSHSVVQQP CCCCCCCCCCCCCCC	16.89	23186163
833	Phosphorylation	PVMSRSHSVVQQPES CCCCCCCCCCCCCCC	25.82	23312004
840	Phosphorylation	SVVQQPESPVYVGHP CCCCCCCCCEECCCE	26.75	18202719
843	Phosphorylation	QQPESPVYVGHPVSV CCCCCCEECCCEEEE	12.23	28464451
849	Phosphorylation	VYVGHPVSVVKLHQS EECCCEEEEEEEECC	26.16	27251275
856	Phosphorylation	SVVKLHQSPVPVTPK EEEEEECCCCCCCCH	19.67	25159151
861	Phosphorylation	HQSPVPVTPKSIQRT ECCCCCCCCHHHHHH	20.94	27732954
876	Phosphorylation	HRETFFKTPGSLGDP HHHHHCCCCCCCCCH	27.94	25850435
879	Phosphorylation	TFFKTPGSLGDPVLK HHCCCCCCCCCHHHH	30.31	24850871
896	Phosphorylation	ERNQSRNTSSAQRRL HHHHCCCCCHHHHHH	23.97	29485707

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

Oops, there are no upstream regulatory protein records of E2F7_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of E2F7_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 E2F7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E2F7_HUMAN	E2F7	physical	14633988
E2F7_HUMAN	E2F7	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-95, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-410, AND MASSSPECTROMETRY.
PubMed: 18669648