dbPTM

EAPP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAPP_HUMAN
UniProt AC	Q56P03
Protein Name	E2F-associated phosphoprotein
Gene Name	EAPP
Organism	Homo sapiens (Human).
Sequence Length	285
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression..
Protein Sequence	MNRLPDDYDPYAVEEPSDEEPALSSSEDEVDVLLHGTPDQKRKLIRECLTGESESSSEDEFEKEMEAELNSTMKTMEDKLSSLGTGSSSGNGKVATAPTRYYDDIYFDSDSEDEDRAVQVTKKKKKKQHKIPTNDELLYDPEKDNRDQAWVDAQRRGYHGLGPQRSRQQQPVPNSDAVLNCPACMTTLCLDCQRHESYKTQYRAMFVMNCSINKEEVLRYKASENRKKRRVHKKMRSNREDAAEKAETDVEEIYHPVMCTECSTEVAVYDKDEVFHFFNVLASHS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNRLPDDY -------CCCCCCCC	6.25	20068231
8	Phosphorylation	MNRLPDDYDPYAVEE CCCCCCCCCCCCCCC	26.63	20068231
11	Phosphorylation	LPDDYDPYAVEEPSD CCCCCCCCCCCCCCC	22.00	20068231
17	Phosphorylation	PYAVEEPSDEEPALS CCCCCCCCCCCCCCC	62.02	25137130
24	Phosphorylation	SDEEPALSSSEDEVD CCCCCCCCCCCCHHH	33.64	25137130
25	Phosphorylation	DEEPALSSSEDEVDV CCCCCCCCCCCHHHH	38.30	25137130
26	Phosphorylation	EEPALSSSEDEVDVL CCCCCCCCCCHHHHH	45.77	25137130
29	Ubiquitination	ALSSSEDEVDVLLHG CCCCCCCHHHHHHCC	36.24	21890473
37	Phosphorylation	VDVLLHGTPDQKRKL HHHHHCCCHHHHHHH	16.97	25137130
50	Phosphorylation	KLIRECLTGESESSS HHHHHHHCCCCCCCC	51.03	17081983
53	Phosphorylation	RECLTGESESSSEDE HHHHCCCCCCCCHHH	44.09	28102081
55	Phosphorylation	CLTGESESSSEDEFE HHCCCCCCCCHHHHH	48.74	25159151
56	Phosphorylation	LTGESESSSEDEFEK HCCCCCCCCHHHHHH	33.42	25159151
57	Phosphorylation	TGESESSSEDEFEKE CCCCCCCCHHHHHHH	59.34	25159151
58	Ubiquitination	GESESSSEDEFEKEM CCCCCCCHHHHHHHH	64.60	27667366
71	Phosphorylation	EMEAELNSTMKTMED HHHHHHHHHHHHHHH	42.37	26552605
72	Phosphorylation	MEAELNSTMKTMEDK HHHHHHHHHHHHHHH	22.93	26552605
79	Ubiquitination	TMKTMEDKLSSLGTG HHHHHHHHHHHCCCC	36.64	29967540
79	Sumoylation	TMKTMEDKLSSLGTG HHHHHHHHHHHCCCC	36.64	-
79	Sumoylation	TMKTMEDKLSSLGTG HHHHHHHHHHHCCCC	36.64	-
81	Phosphorylation	KTMEDKLSSLGTGSS HHHHHHHHHCCCCCC	29.29	-
82	Phosphorylation	TMEDKLSSLGTGSSS HHHHHHHHCCCCCCC	41.05	19413330
85	Phosphorylation	DKLSSLGTGSSSGNG HHHHHCCCCCCCCCC	38.90	22199227
87	Phosphorylation	LSSLGTGSSSGNGKV HHHCCCCCCCCCCCC	22.59	25849741
88	Phosphorylation	SSLGTGSSSGNGKVA HHCCCCCCCCCCCCC	43.54	22199227
89	Phosphorylation	SLGTGSSSGNGKVAT HCCCCCCCCCCCCCC	37.67	21815630
93	Sumoylation	GSSSGNGKVATAPTR CCCCCCCCCCCCCCE	32.47	-
93	Ubiquitination	GSSSGNGKVATAPTR CCCCCCCCCCCCCCE	32.47	27667366
93	Sumoylation	GSSSGNGKVATAPTR CCCCCCCCCCCCCCE	32.47	-
96	Phosphorylation	SGNGKVATAPTRYYD CCCCCCCCCCCEEEC	35.84	28796482
99	Phosphorylation	GKVATAPTRYYDDIY CCCCCCCCEEECEEE	28.92	28796482
101	Phosphorylation	VATAPTRYYDDIYFD CCCCCCEEECEEECC	17.45	28796482
102	Phosphorylation	ATAPTRYYDDIYFDS CCCCCEEECEEECCC	12.12	28796482
106	Phosphorylation	TRYYDDIYFDSDSED CEEECEEECCCCCCC	14.34	22167270
109	Phosphorylation	YDDIYFDSDSEDEDR ECEEECCCCCCCCHH	32.89	22167270
111	Phosphorylation	DIYFDSDSEDEDRAV EEECCCCCCCCHHHH	51.39	22167270
121	Phosphorylation	EDRAVQVTKKKKKKQ CHHHHHHHHHHCCCC	21.76	23927012
122	Ubiquitination	DRAVQVTKKKKKKQH HHHHHHHHHHCCCCC	64.83	27667366
130	Sumoylation	KKKKKQHKIPTNDEL HHCCCCCCCCCCCCC	48.14	-
130	Ubiquitination	KKKKKQHKIPTNDEL HHCCCCCCCCCCCCC	48.14	29967540
130	Sumoylation	KKKKKQHKIPTNDEL HHCCCCCCCCCCCCC	48.14	-
139	Phosphorylation	PTNDELLYDPEKDNR CCCCCCCCCCCCCCC	41.92	21945579
143	Ubiquitination	ELLYDPEKDNRDQAW CCCCCCCCCCCCHHH	66.74	29967540
158	Phosphorylation	VDAQRRGYHGLGPQR HHHHHCCCCCCCCCC	7.30	24043423
166	Phosphorylation	HGLGPQRSRQQQPVP CCCCCCCCCCCCCCC	29.24	24043423
220	Phosphorylation	NKEEVLRYKASENRK CHHHHHHHHHCCCHH	13.52	23532336

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U520_HUMAN	SNRNP200	physical	26186194
GPTC1_HUMAN	GPATCH1	physical	26186194
DHX35_HUMAN	DHX35	physical	26186194
AAR2_HUMAN	AAR2	physical	26186194
ECD_HUMAN	ECD	physical	26186194
CDC5L_HUMAN	CDC5L	physical	26186194
CRNL1_HUMAN	CRNKL1	physical	26186194
WDR83_HUMAN	WDR83	physical	26186194
AAR2_HUMAN	AAR2	physical	26344197
AAR2_HUMAN	AAR2	physical	28514442
ECD_HUMAN	ECD	physical	28514442
CD2B2_HUMAN	CD2BP2	physical	28514442
GPTC1_HUMAN	GPATCH1	physical	28514442
DHX35_HUMAN	DHX35	physical	28514442
WDR83_HUMAN	WDR83	physical	28514442
U520_HUMAN	SNRNP200	physical	28514442
PRP8_HUMAN	PRPF8	physical	28514442
U5S1_HUMAN	EFTUD2	physical	28514442
AAR2_HUMAN	AAR2	physical	28561026
AQR_HUMAN	AQR	physical	28561026
CD2B2_HUMAN	CD2BP2	physical	28561026
CDC5L_HUMAN	CDC5L	physical	28561026
CWC22_HUMAN	CWC22	physical	28561026
DDX23_HUMAN	DDX23	physical	28561026
PRP16_HUMAN	DHX38	physical	28561026
DHX8_HUMAN	DHX8	physical	28561026
EAPP_HUMAN	EAPP	physical	28561026
ECD_HUMAN	ECD	physical	28561026
U5S1_HUMAN	EFTUD2	physical	28561026
HSF1_HUMAN	HSF1	physical	28561026
ISY1_HUMAN	ISY1	physical	28561026
NCDN_HUMAN	NCDN	physical	28561026
PLRG1_HUMAN	PLRG1	physical	28561026
PRP19_HUMAN	PRPF19	physical	28561026
PRP6_HUMAN	PRPF6	physical	28561026
PRP8_HUMAN	PRPF8	physical	28561026
RUVB1_HUMAN	RUVBL1	physical	28561026
RUVB2_HUMAN	RUVBL2	physical	28561026
SLU7_HUMAN	SLU7	physical	28561026
SMYD4_HUMAN	SMYD4	physical	28561026
U520_HUMAN	SNRNP200	physical	28561026
RSMB_HUMAN	SNRPB	physical	28561026
SMD1_HUMAN	SNRPD1	physical	28561026
SMD2_HUMAN	SNRPD2	physical	28561026
SMD3_HUMAN	SNRPD3	physical	28561026
RUXE_HUMAN	SNRPE	physical	28561026
SNW1_HUMAN	SNW1	physical	28561026
SRRM2_HUMAN	SRRM2	physical	28561026
TSSC4_HUMAN	TSSC4	physical	28561026
SYF1_HUMAN	XAB2	physical	28561026
ZNHI2_HUMAN	ZNHIT2	physical	28561026
SNUT2_HUMAN	USP39	physical	28561026

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 EAPP_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-109 AND SER-111, ANDMASS SPECTROMETRY.	19690332 [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-109 AND SER-111, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-24; SER-25;SER-26; THR-37; THR-50; SER-53; SER-55; SER-56; SER-57; SER-109 ANDSER-111, AND MASS SPECTROMETRY.	17081983 [Abstract]