dbPTM

EDC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EDC3_HUMAN
UniProt AC	Q96F86
Protein Name	Enhancer of mRNA-decapping protein 3
Gene Name	EDC3
Organism	Homo sapiens (Human).
Sequence Length	508
Subcellular Localization	Cytoplasm, P-body . Processing bodies (PB).
Protein Description	Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis..
Protein Sequence	MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGTGKFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKDLPTSPVDLVINCLDCPENVFLRDQPWYKAAVAWANQNRAPVLSIDPPVHEVEQGIDAKWSLALGLPLPLGEHAGRIYLCDIGIPQQVFQEVGINYHSPFGCKFVIPLHSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	IVSINCGDSLGVYQG EEEEECCCCCEECCC	42.78	32645325
36	Phosphorylation	DQVSQTISLTRPFHN HHHHCEEECCCCCCC	27.37	24719451
47	Glutathionylation	PFHNGVKCLVPEVTF CCCCCEEEECEEEEE	4.26	22555962
100	Phosphorylation	VGINQNGTGKFVKKP EEECCCCCCCEEECC	44.76	-
102	Acetylation	INQNGTGKFVKKPAS ECCCCCCCEEECCCC	46.99	25953088
105	Ubiquitination	NGTGKFVKKPASSSS CCCCCEEECCCCCCC	57.05	29967540
106	Ubiquitination	GTGKFVKKPASSSSA CCCCEEECCCCCCCC	40.28	29967540
109	Phosphorylation	KFVKKPASSSSAPQN CEEECCCCCCCCCCC	39.00	30206219
110	Phosphorylation	FVKKPASSSSAPQNI EEECCCCCCCCCCCC	30.34	30206219
111	Phosphorylation	VKKPASSSSAPQNIP EECCCCCCCCCCCCC	28.20	30576142
112	Phosphorylation	KKPASSSSAPQNIPK ECCCCCCCCCCCCCC	46.01	25159151
119	Ubiquitination	SAPQNIPKRTDVKSQ CCCCCCCCCCCCCCC	65.22	29967540
121	Phosphorylation	PQNIPKRTDVKSQDV CCCCCCCCCCCCCCC	51.80	28111955
125	Phosphorylation	PKRTDVKSQDVAVSP CCCCCCCCCCCCCCH	31.31	22167270
131	Phosphorylation	KSQDVAVSPQQQQCS CCCCCCCCHHHHHHC	13.78	19664994
138	Phosphorylation	SPQQQQCSKSYVDRH CHHHHHHCHHHHHHH	21.94	22167270
139	Methylation	PQQQQCSKSYVDRHM HHHHHHCHHHHHHHH	54.13	-
140	Phosphorylation	QQQQCSKSYVDRHME HHHHHCHHHHHHHHH	17.69	25159151
141	Phosphorylation	QQQCSKSYVDRHMES HHHHCHHHHHHHHHH	15.31	30576142
144	Methylation	CSKSYVDRHMESLSQ HCHHHHHHHHHHHHC	22.47	-
148	Phosphorylation	YVDRHMESLSQSKSF HHHHHHHHHHCCHHH	26.25	22496350
150	Phosphorylation	DRHMESLSQSKSFRR HHHHHHHHCCHHHHH	41.51	25159151
152	Phosphorylation	HMESLSQSKSFRRRH HHHHHHCCHHHHHHH	27.22	22496350
153	Ubiquitination	MESLSQSKSFRRRHN HHHHHCCHHHHHHHC	46.07	29967540
154	Phosphorylation	ESLSQSKSFRRRHNS HHHHCCHHHHHHHCC	29.27	23401153
161	Phosphorylation	SFRRRHNSWSSSSRH HHHHHHCCCCCCCCC	23.39	22617229
163	Phosphorylation	RRRHNSWSSSSRHPN HHHHCCCCCCCCCCC	21.84	27273156
164	Phosphorylation	RRHNSWSSSSRHPNQ HHHCCCCCCCCCCCC	26.52	20201521
165	Phosphorylation	RHNSWSSSSRHPNQA HHCCCCCCCCCCCCC	26.35	22115753
166	Phosphorylation	HNSWSSSSRHPNQAT HCCCCCCCCCCCCCC	36.23	22617229
173	Phosphorylation	SRHPNQATPKKSGLK CCCCCCCCCCCCCCC	26.36	26055452
175	Ubiquitination	HPNQATPKKSGLKNG CCCCCCCCCCCCCCC	56.04	29967540
177	Phosphorylation	NQATPKKSGLKNGQM CCCCCCCCCCCCCCC	56.32	26425664
224	Phosphorylation	AVFEEIDTYERRSGT HHEEECCCCCCCCCC	32.70	28796482
225	Phosphorylation	VFEEIDTYERRSGTR HEEECCCCCCCCCCC	12.04	28796482
233	Phosphorylation	ERRSGTRSRGIPNER CCCCCCCCCCCCCCC	34.40	27067055
234	Methylation	RRSGTRSRGIPNERP CCCCCCCCCCCCCCC	43.71	-
243	Ubiquitination	IPNERPTRYRHDENI CCCCCCCCCCCCCCC	29.21	21890473
253	Phosphorylation	HDENILESEPIVYRR CCCCCCCCCCEEEEE	45.27	25867546
258	Phosphorylation	LESEPIVYRRIIVPH CCCCCEEEEEEECCC	8.56	17360941
269	Acetylation	IVPHNVSKEFCTDSG ECCCCCCHHHCCCCC	50.99	26051181
269	Ubiquitination	IVPHNVSKEFCTDSG ECCCCCCHHHCCCCC	50.99	-
288	Ubiquitination	SISYELHKKLLSVAE EECHHHHHHHHHHHH	58.71	29967540
289	Ubiquitination	ISYELHKKLLSVAEK ECHHHHHHHHHHHHH	43.86	29967540
296	Ubiquitination	KLLSVAEKHGLTLER HHHHHHHHCCCCHHH	32.98	29967540
296	Acetylation	KLLSVAEKHGLTLER HHHHHHHHCCCCHHH	32.98	26051181
300	Phosphorylation	VAEKHGLTLERRLEM HHHHCCCCHHHHHHH	31.03	-
308	Phosphorylation	LERRLEMTGVCASQM HHHHHHHHHHHHHHH	19.65	20068231
313	Phosphorylation	EMTGVCASQMALTLL HHHHHHHHHHHHHHH	18.50	20068231
318	Phosphorylation	CASQMALTLLGGPNR HHHHHHHHHHCCCCC	15.48	20068231
346	Malonylation	LLCGPHVKGAQGISC EEECCCCCCCCCCCC	45.56	26320211
346	Acetylation	LLCGPHVKGAQGISC EEECCCCCCCCCCCC	45.56	26051181
383	Phosphorylation	ESITNELSLFSKTQG HHHHHHHHHHHCCCC	22.61	20068231
386	Phosphorylation	TNELSLFSKTQGQQV HHHHHHHHCCCCCCC	39.83	20068231
387	Ubiquitination	NELSLFSKTQGQQVS HHHHHHHCCCCCCCC	37.22	29967540
394	Phosphorylation	KTQGQQVSSLKDLPT CCCCCCCCCCCCCCC	26.14	22617229
426	Ubiquitination	LRDQPWYKAAVAWAN CCCCHHHHHHHHHHH	26.46	22817900
507	Phosphorylation	KFVIPLHSA------ EEEEECCCC------	43.27	27067055

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
161	S	Phosphorylation	Kinase	AKT1	P31749	PSP
161	S	Phosphorylation	Kinase	AKT2	P31751	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EDC3_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 EDC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EDC4_HUMAN	EDC4	physical	16364915
DCP1A_HUMAN	DCP1A	physical	16364915
DDX6_HUMAN	DDX6	physical	16364915
DCP2_HUMAN	DCP2	physical	16364915
EDC3_HUMAN	EDC3	physical	25416956
EFHC2_HUMAN	EFHC2	physical	25416956
DCP1B_HUMAN	DCP1B	physical	25416956
DCP1B_HUMAN	DCP1B	physical	26186194
DCP1A_HUMAN	DCP1A	physical	26186194
DCP1B_HUMAN	DCP1B	physical	28514442
BAG4_HUMAN	BAG4	physical	28514442
DCP1A_HUMAN	DCP1A	physical	28514442
KCTD3_HUMAN	KCTD3	physical	27173435
KI13B_HUMAN	KIF13B	physical	27173435
ZBT21_HUMAN	ZBTB21	physical	27173435
KSR1_HUMAN	KSR1	physical	27173435
GGYF1_HUMAN	GIGYF1	physical	27173435
LRFN1_HUMAN	LRFN1	physical	27173435
DEN1A_HUMAN	DENND1A	physical	27173435
SPD2A_HUMAN	SH3PXD2A	physical	27173435
SRGP2_HUMAN	SRGAP2	physical	27173435
IF4E2_HUMAN	EIF4E2	physical	27173435
SI1L1_HUMAN	SIPA1L1	physical	27173435
LIMA1_HUMAN	LIMA1	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
TESK2_HUMAN	TESK2	physical	27173435
DCLK1_HUMAN	DCLK1	physical	27173435
ZN638_HUMAN	ZNF638	physical	27173435
SRS12_HUMAN	SRSF12	physical	27173435
SYDE1_HUMAN	SYDE1	physical	27173435
AGAP1_HUMAN	AGAP1	physical	27173435
MPIP2_HUMAN	CDC25B	physical	27173435
CDK16_HUMAN	CDK16	physical	27173435
CBY1_HUMAN	CBY1	physical	27173435
RAB3I_HUMAN	RAB3IP	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 EDC3_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-161, 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-131, 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-131, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.	16964243 [Abstract]