dbPTM

EDC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EDC4_HUMAN
UniProt AC	Q6P2E9
Protein Name	Enhancer of mRNA-decapping protein 4
Gene Name	EDC4
Organism	Homo sapiens (Human).
Sequence Length	1401
Subcellular Localization	Cytoplasm, P-body . Nucleus .
Protein Description	In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro)..
Protein Sequence	MASCASIDIEDATQHLRDILKLDRPAGGPSAESPRPSSAYNGDLNGLLVPDPLCSGDSTSANKTGLRTMPPINLQEKQVICLSGDDSSTCIGILAKEVEIVASSDSSISSKARGSNKVKIQPVAKYDWEQKYYYGNLIAVSNSFLAYAIRAANNGSAMVRVISVSTSERTLLKGFTGSVADLAFAHLNSPQLACLDEAGNLFVWRLALVNGKIQEEILVHIRQPEGTPLNHFRRIIWCPFIPEESEDCCEESSPTVALLHEDRAEVWDLDMLRSSHSTWPVDVSQIKQGFIVVKGHSTCLSEGALSPDGTVLATASHDGYVKFWQIYIEGQDEPRCLHEWKPHDGRPLSCLLFCDNHKKQDPDVPFWRFLITGADQNRELKMWCTVSWTCLQTIRFSPDIFSSVSVPPSLKVCLDLSAEYLILSDVQRKVLYVMELLQNQEEGHACFSSISEFLLTHPVLSFGIQVVSRCRLRHTEVLPAEEENDSLGADGTHGAGAMESAAGVLIKLFCVHTKALQDVQIRFQPQLNPDVVAPLPTHTAHEDFTFGESRPELGSEGLGSAAHGSQPDLRRIVELPAPADFLSLSSETKPKLMTPDAFMTPSASLQQITASPSSSSSGSSSSSSSSSSSLTAVSAMSSTSAVDPSLTRPPEELTLSPKLQLDGSLTMSSSGSLQASPRGLLPGLLPAPADKLTPKGPGQVPTATSALSLELQEVEPLGLPQASPSRTRSPDVISSASTALSQDIPEIASEALSRGFGSSAPEGLEPDSMASAASALHLLSPRPRPGPELGPQLGLDGGPGDGDRHNTPSLLEAALTQEASTPDSQVWPTAPDITRETCSTLAESPRNGLQEKHKSLAFHRPPYHLLQQRDSQDASAEQSDHDDEVASLASASGGFGTKVPAPRLPAKDWKTKGSPRTSPKLKRKSKKDDGDAAMGSRLTEHQVAEPPEDWPALIWQQQRELAELRHSQEELLQRLCTQLEGLQSTVTGHVERALETRHEQEQRRLERALAEGQQRGGQLQEQLTQQLSQALSSAVAGRLERSIRDEIKKTVPPCVSRSLEPMAGQLSNSVATKLTAVEGSMKENISKLLKSKNLTDAIARAAADTLQGPMQAAYREAFQSVVLPAFEKSCQAMFQQINDSFRLGTQEYLQQLESHMKSRKAREQEAREPVLAQLRGLVSTLQSATEQMAATVAGSVRAEVQHQLHVAVGSLQESILAQVQRIVKGEVSVALKEQQAAVTSSIMQAMRSAAGTPVPSAHLDCQAQQAHILQLLQQGHLNQAFQQALTAADLNLVLYVCETVDPAQVFGQPPCPLSQPVLLSLIQQLASDLGTRTDLKLSYLEEAVMHLDHSDPITRDHMGSVMAQVRQKLFQFLQAEPHNSLGKAARRLSLMLHGLVTPSLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASCASIDI ------CCCCCCCCH	25.31	19413330
3	Phosphorylation	-----MASCASIDIE -----CCCCCCCCHH	23.29	28122231
6	Phosphorylation	--MASCASIDIEDAT --CCCCCCCCHHHHH	25.72	25159151
13	Phosphorylation	SIDIEDATQHLRDIL CCCHHHHHHHHHHHH	28.92	26552605
21	Ubiquitination	QHLRDILKLDRPAGG HHHHHHHHCCCCCCC	48.99	29967540
30	Phosphorylation	DRPAGGPSAESPRPS CCCCCCCCCCCCCCC	48.20	23401153
33	Phosphorylation	AGGPSAESPRPSSAY CCCCCCCCCCCCCCC	26.40	29255136
37	Phosphorylation	SAESPRPSSAYNGDL CCCCCCCCCCCCCCC	28.96	25159151
38	Phosphorylation	AESPRPSSAYNGDLN CCCCCCCCCCCCCCC	37.14	30576142
40	Phosphorylation	SPRPSSAYNGDLNGL CCCCCCCCCCCCCCE	22.94	30576142
55	Phosphorylation	LVPDPLCSGDSTSAN ECCCCCCCCCCCCCC	54.00	20068231
58	Phosphorylation	DPLCSGDSTSANKTG CCCCCCCCCCCCCCC	27.99	20068231
59	Phosphorylation	PLCSGDSTSANKTGL CCCCCCCCCCCCCCC	36.28	20068231
60	Phosphorylation	LCSGDSTSANKTGLR CCCCCCCCCCCCCCC	33.52	25159151
63	Ubiquitination	GDSTSANKTGLRTMP CCCCCCCCCCCCCCC	43.62	29967540
64	Phosphorylation	DSTSANKTGLRTMPP CCCCCCCCCCCCCCC	41.05	23312004
103	Phosphorylation	KEVEIVASSDSSISS EEEEEEECCCCCCCC	24.63	20068231
104	Phosphorylation	EVEIVASSDSSISSK EEEEEECCCCCCCCC	31.60	20068231
106	Phosphorylation	EIVASSDSSISSKAR EEEECCCCCCCCCCC	31.36	20068231
107	Phosphorylation	IVASSDSSISSKARG EEECCCCCCCCCCCC	31.32	20068231
109	Phosphorylation	ASSDSSISSKARGSN ECCCCCCCCCCCCCC	27.95	20068231
110	Phosphorylation	SSDSSISSKARGSNK CCCCCCCCCCCCCCC	28.76	20068231
111	Ubiquitination	SDSSISSKARGSNKV CCCCCCCCCCCCCCC	35.00	32015554
119	Ubiquitination	ARGSNKVKIQPVAKY CCCCCCCEEEECEEC	36.91	29967540
125	Acetylation	VKIQPVAKYDWEQKY CEEEECEECCHHHCE	43.93	19608861
125	Ubiquitination	VKIQPVAKYDWEQKY CEEEECEECCHHHCE	43.93	22817900
125 (in isoform 1)	Ubiquitination	-	43.93	21890473
126	Phosphorylation	KIQPVAKYDWEQKYY EEEECEECCHHHCEE	19.29	22817900
147	Phosphorylation	VSNSFLAYAIRAANN ECHHHHHHHHHHHHC	12.52	22817900
165	Phosphorylation	MVRVISVSTSERTLL EEEEEEEECCCCHHH	21.30	22210691
166	Phosphorylation	VRVISVSTSERTLLK EEEEEEECCCCHHHC	32.24	22210691
170	Phosphorylation	SVSTSERTLLKGFTG EEECCCCHHHCCCCC	32.18	22210691
287	Ubiquitination	PVDVSQIKQGFIVVK CCCHHHCCCCEEEEE	36.41	-
359	Ubiquitination	LFCDNHKKQDPDVPF EEECCCCCCCCCCCH	53.00	29967540
385	Phosphorylation	RELKMWCTVSWTCLQ CEEEHHHEEEHHHHH	11.32	24043423
387	Phosphorylation	LKMWCTVSWTCLQTI EEHHHEEEHHHHHHH	9.87	24043423
389	Phosphorylation	MWCTVSWTCLQTIRF HHHEEEHHHHHHHCC	8.88	24043423
393	Phosphorylation	VSWTCLQTIRFSPDI EEHHHHHHHCCCCCH	10.94	24043423
405	Phosphorylation	PDIFSSVSVPPSLKV CCHHHCCCCCCCHHH	30.74	-
409	Phosphorylation	SSVSVPPSLKVCLDL HCCCCCCCHHHHHHH	34.45	20068231
475	Phosphorylation	SRCRLRHTEVLPAEE HCCCCCCCEEECCHH	22.73	20068231
486	Phosphorylation	PAEEENDSLGADGTH CCHHHCCCCCCCCCC	40.04	23401153
492	Phosphorylation	DSLGADGTHGAGAME CCCCCCCCCCHHHHH	20.06	28192239
500	Phosphorylation	HGAGAMESAAGVLIK CCHHHHHHHHHHHHH	15.44	23401153
514	Acetylation	KLFCVHTKALQDVQI HHHHHHCCHHCCCHH	32.02	26051181
537	Phosphorylation	DVVAPLPTHTAHEDF CCEECCCCCCCCCCC	39.27	26330541
539	Phosphorylation	VAPLPTHTAHEDFTF EECCCCCCCCCCCCC	31.99	26330541
545	Phosphorylation	HTAHEDFTFGESRPE CCCCCCCCCCCCCCC	42.95	26074081
549	Phosphorylation	EDFTFGESRPELGSE CCCCCCCCCCCCCCC	54.22	26074081
555	Phosphorylation	ESRPELGSEGLGSAA CCCCCCCCCCCCHHC	40.91	29255136
560	Phosphorylation	LGSEGLGSAAHGSQP CCCCCCCHHCCCCCC	27.59	29255136
565	Phosphorylation	LGSAAHGSQPDLRRI CCHHCCCCCCCHHHH	28.77	29255136
583	Phosphorylation	PAPADFLSLSSETKP CCCCCHHCCCCCCCC	26.63	24972180
585	Phosphorylation	PADFLSLSSETKPKL CCCHHCCCCCCCCCC	23.81	25159151
586	Phosphorylation	ADFLSLSSETKPKLM CCHHCCCCCCCCCCC	55.36	26055452
588	Phosphorylation	FLSLSSETKPKLMTP HHCCCCCCCCCCCCC	55.37	25159151
589	Acetylation	LSLSSETKPKLMTPD HCCCCCCCCCCCCCC	35.78	26051181
589	Ubiquitination	LSLSSETKPKLMTPD HCCCCCCCCCCCCCC	35.78	-
594	Phosphorylation	ETKPKLMTPDAFMTP CCCCCCCCCCCCCCC	28.58	26074081
613	Phosphorylation	QQITASPSSSSSGSS HHHHCCCCCCCCCCC	40.12	-
621	Phosphorylation	SSSSGSSSSSSSSSS CCCCCCCCCCCCCCC	35.62	-
622	Phosphorylation	SSSGSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
623	Phosphorylation	SSGSSSSSSSSSSSL CCCCCCCCCCCCCCC	35.87	-
624	Phosphorylation	SGSSSSSSSSSSSLT CCCCCCCCCCCCCCH	35.87	-
640	O-linked_Glycosylation	VSAMSSTSAVDPSLT HHCCCCCCCCCHHHC	28.39	OGP
645	Phosphorylation	STSAVDPSLTRPPEE CCCCCCHHHCCCCHH	37.60	21406692
647	Phosphorylation	SAVDPSLTRPPEELT CCCCHHHCCCCHHCC	45.53	21406692
654	Phosphorylation	TRPPEELTLSPKLQL CCCCHHCCCCCCEEE	28.59	26074081
656	Phosphorylation	PPEELTLSPKLQLDG CCHHCCCCCCEEECC	18.11	26657352
664	Phosphorylation	PKLQLDGSLTMSSSG CCEEECCCEEECCCC	21.97	26055452
666	Phosphorylation	LQLDGSLTMSSSGSL EEECCCEEECCCCCC	19.39	27732954
668	Phosphorylation	LDGSLTMSSSGSLQA ECCCEEECCCCCCCC	19.00	22199227
669	Phosphorylation	DGSLTMSSSGSLQAS CCCEEECCCCCCCCC	28.09	22199227
670	Phosphorylation	GSLTMSSSGSLQASP CCEEECCCCCCCCCC	25.70	22199227
672	Phosphorylation	LTMSSSGSLQASPRG EEECCCCCCCCCCCC	21.18	22199227
676	Phosphorylation	SSGSLQASPRGLLPG CCCCCCCCCCCCCCC	11.36	25159151
691	Acetylation	LLPAPADKLTPKGPG CCCCCHHHCCCCCCC	57.26	25953088
693	Phosphorylation	PAPADKLTPKGPGQV CCCHHHCCCCCCCCC	28.79	30266825
702	Phosphorylation	KGPGQVPTATSALSL CCCCCCCCHHHEEEE	43.65	30278072
704	Phosphorylation	PGQVPTATSALSLEL CCCCCCHHHEEEEEE	19.60	28176443
705	Phosphorylation	GQVPTATSALSLELQ CCCCCHHHEEEEEEE	25.42	28176443
708	Phosphorylation	PTATSALSLELQEVE CCHHHEEEEEEEECC	21.36	30278072
723	Phosphorylation	PLGLPQASPSRTRSP CCCCCCCCCCCCCCH	20.40	29255136
725	Phosphorylation	GLPQASPSRTRSPDV CCCCCCCCCCCCHHH	43.73	29255136
727	Phosphorylation	PQASPSRTRSPDVIS CCCCCCCCCCHHHHH	39.58	22167270
729	Phosphorylation	ASPSRTRSPDVISSA CCCCCCCCHHHHHHH	25.49	19664994
734	Phosphorylation	TRSPDVISSASTALS CCCHHHHHHHHHHHH	21.50	22167270
735	Phosphorylation	RSPDVISSASTALSQ CCHHHHHHHHHHHHC	18.34	26846344
737	Phosphorylation	PDVISSASTALSQDI HHHHHHHHHHHHCCH	19.03	26846344
738	Phosphorylation	DVISSASTALSQDIP HHHHHHHHHHHCCHH	31.19	26846344
741	Phosphorylation	SSASTALSQDIPEIA HHHHHHHHCCHHHHH	24.28	26846344
749	Phosphorylation	QDIPEIASEALSRGF CCHHHHHHHHHHCCC	29.12	23927012
753	Phosphorylation	EIASEALSRGFGSSA HHHHHHHHCCCCCCC	37.09	23927012
758	Phosphorylation	ALSRGFGSSAPEGLE HHHCCCCCCCCCCCC	22.52	25850435
759	Phosphorylation	LSRGFGSSAPEGLEP HHCCCCCCCCCCCCC	48.50	25850435
768	Phosphorylation	PEGLEPDSMASAASA CCCCCCCHHHHHHHH	27.28	27794612
771	Phosphorylation	LEPDSMASAASALHL CCCCHHHHHHHHHHH	18.74	27794612
774	Phosphorylation	DSMASAASALHLLSP CHHHHHHHHHHHHCC	30.95	26055452
780	Phosphorylation	ASALHLLSPRPRPGP HHHHHHHCCCCCCCC	25.81	29255136
807	Phosphorylation	GDGDRHNTPSLLEAA CCCCCCCCHHHHHHH	14.23	26055452
809	Phosphorylation	GDRHNTPSLLEAALT CCCCCCHHHHHHHHH	43.48	21712546
816	Phosphorylation	SLLEAALTQEASTPD HHHHHHHHHCCCCCC	21.45	20873877
820	Phosphorylation	AALTQEASTPDSQVW HHHHHCCCCCCHHHC	39.46	25159151
821	Phosphorylation	ALTQEASTPDSQVWP HHHHCCCCCCHHHCC	37.86	25159151
824	Phosphorylation	QEASTPDSQVWPTAP HCCCCCCHHHCCCCC	28.04	20873877
829	Phosphorylation	PDSQVWPTAPDITRE CCHHHCCCCCCCCHH	34.80	20068231
834	Phosphorylation	WPTAPDITRETCSTL CCCCCCCCHHHHHHH	29.81	20068231
837	Phosphorylation	APDITRETCSTLAES CCCCCHHHHHHHHHC	14.41	23898821
839	Phosphorylation	DITRETCSTLAESPR CCCHHHHHHHHHCCC	33.60	25159151
840	Phosphorylation	ITRETCSTLAESPRN CCHHHHHHHHHCCCC	31.94	30266825
844	Phosphorylation	TCSTLAESPRNGLQE HHHHHHHCCCCCHHH	24.45	19664994
855	Phosphorylation	GLQEKHKSLAFHRPP CHHHHHHHHHHCCCC	25.34	28348404
863	Phosphorylation	LAFHRPPYHLLQQRD HHHCCCCHHHHCCCC	14.05	28796482
871	Phosphorylation	HLLQQRDSQDASAEQ HHHCCCCCCCCCHHH	31.95	23927012
875	Phosphorylation	QRDSQDASAEQSDHD CCCCCCCCHHHCCCH	40.40	20201521
879	Phosphorylation	QDASAEQSDHDDEVA CCCCHHHCCCHHHHH	28.55	20201521
887	Phosphorylation	DHDDEVASLASASGG CCHHHHHHHHHHCCC	29.64	23927012
887 (in isoform 2)	Ubiquitination	-	29.64	21906983
890	Phosphorylation	DEVASLASASGGFGT HHHHHHHHHCCCCCC	28.41	30278072
892	Phosphorylation	VASLASASGGFGTKV HHHHHHHCCCCCCCC	36.63	23927012
897	Phosphorylation	SASGGFGTKVPAPRL HHCCCCCCCCCCCCC	26.97	23927012
907	Acetylation	PAPRLPAKDWKTKGS CCCCCCCCCCCCCCC	63.28	25953088
911	Phosphorylation	LPAKDWKTKGSPRTS CCCCCCCCCCCCCCC	36.06	20363803
914	Phosphorylation	KDWKTKGSPRTSPKL CCCCCCCCCCCCHHH	16.86	28102081
917	Phosphorylation	KTKGSPRTSPKLKRK CCCCCCCCCHHHCCC	53.41	30576142
918	Phosphorylation	TKGSPRTSPKLKRKS CCCCCCCCHHHCCCC	22.71	28102081
925	Phosphorylation	SPKLKRKSKKDDGDA CHHHCCCCCCCCCCC	49.31	21406692
926	Ubiquitination	PKLKRKSKKDDGDAA HHHCCCCCCCCCCCC	64.36	24816145
936	Phosphorylation	DGDAAMGSRLTEHQV CCCCCHHCCCCCCCC	15.84	21406692
965	Methylation	QRELAELRHSQEELL HHHHHHHHHCHHHHH	20.93	-
967	Phosphorylation	ELAELRHSQEELLQR HHHHHHHCHHHHHHH	32.62	20873877
977	Phosphorylation	ELLQRLCTQLEGLQS HHHHHHHHHHHHHHH	40.56	24719451
1015	Methylation	ALAEGQQRGGQLQEQ HHHHHHHHHHHHHHH	43.23	-
1042	Phosphorylation	VAGRLERSIRDEIKK HHHHHHHHHHHHHHH	16.76	23898821
1049	Ubiquitination	SIRDEIKKTVPPCVS HHHHHHHHHCCCCHH	61.49	24816145
1050	Phosphorylation	IRDEIKKTVPPCVSR HHHHHHHHCCCCHHH	32.99	27470641
1058	Phosphorylation	VPPCVSRSLEPMAGQ CCCCHHHCCCCCCHH	29.58	23612710
1062	Sulfoxidation	VSRSLEPMAGQLSNS HHHCCCCCCHHCHHH	4.83	21406390
1067	Phosphorylation	EPMAGQLSNSVATKL CCCCHHCHHHHHHHH	21.12	20068231
1069	Phosphorylation	MAGQLSNSVATKLTA CCHHCHHHHHHHHHH	15.11	20068231
1072	Phosphorylation	QLSNSVATKLTAVEG HCHHHHHHHHHHCCC	25.16	20068231
1075	Phosphorylation	NSVATKLTAVEGSMK HHHHHHHHHCCCHHH	30.16	22673903
1080	Phosphorylation	KLTAVEGSMKENISK HHHHCCCHHHHHHHH	17.11	22673903
1082	Ubiquitination	TAVEGSMKENISKLL HHCCCHHHHHHHHHH	49.67	-
1087	Acetylation	SMKENISKLLKSKNL HHHHHHHHHHHCCCH	54.78	25953088
1087	Malonylation	SMKENISKLLKSKNL HHHHHHHHHHHCCCH	54.78	26320211
1087	Ubiquitination	SMKENISKLLKSKNL HHHHHHHHHHHCCCH	54.78	29967540
1092	2-Hydroxyisobutyrylation	ISKLLKSKNLTDAIA HHHHHHCCCHHHHHH	55.15	-
1092	Malonylation	ISKLLKSKNLTDAIA HHHHHHCCCHHHHHH	55.15	26320211
1092	Ubiquitination	ISKLLKSKNLTDAIA HHHHHHCCCHHHHHH	55.15	29967540
1148	Phosphorylation	FRLGTQEYLQQLESH HHHCHHHHHHHHHHH	10.45	28555341
1154	Phosphorylation	EYLQQLESHMKSRKA HHHHHHHHHHHHHHH	37.16	25159151
1157	Acetylation	QQLESHMKSRKAREQ HHHHHHHHHHHHHHH	41.50	25953088
1157	Ubiquitination	QQLESHMKSRKAREQ HHHHHHHHHHHHHHH	41.50	23000965
1157 (in isoform 1)	Ubiquitination	-	41.50	21890473
1158	Phosphorylation	QLESHMKSRKAREQE HHHHHHHHHHHHHHH	31.29	28857561
1160	Ubiquitination	ESHMKSRKAREQEAR HHHHHHHHHHHHHHH	59.91	23000965
1248	Phosphorylation	SIMQAMRSAAGTPVP HHHHHHHHHCCCCCC	14.91	26657352
1252	Phosphorylation	AMRSAAGTPVPSAHL HHHHHCCCCCCCHHH	19.18	26657352
1256	Phosphorylation	AAGTPVPSAHLDCQA HCCCCCCCHHHHHHH	28.67	26074081
1345	Sulfoxidation	SYLEEAVMHLDHSDP HHHHHHHHCCCCCCC	3.15	30846556
1368	Acetylation	VMAQVRQKLFQFLQA HHHHHHHHHHHHHHC	40.48	26051181
1368	Ubiquitination	VMAQVRQKLFQFLQA HHHHHHHHHHHHHHC	40.48	-
1380	Phosphorylation	LQAEPHNSLGKAARR HHCCCCCHHHHHHHH	35.15	22617229
1383	Ubiquitination	EPHNSLGKAARRLSL CCCCHHHHHHHHHHH	44.13	-
1389	Phosphorylation	GKAARRLSLMLHGLV HHHHHHHHHHHCCCC	15.21	28450419
1399	Phosphorylation	LHGLVTPSLP----- HCCCCCCCCC-----	43.86	27251275

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
107	S	Phosphorylation	Kinase	IKKB	O14920	PSP
405	S	Phosphorylation	Kinase	IKKB	O14920	PSP
583	S	Phosphorylation	Kinase	IKKB	O14920	PSP
855	S	Phosphorylation	Kinase	IKKB	O14920	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EDC4_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 EDC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCP2_HUMAN	DCP2	physical	21672539
DCP1B_HUMAN	DCP1B	physical	21672539
DCP1A_HUMAN	DCP1A	physical	16364915
DCP2_HUMAN	DCP2	physical	16364915
FBLN1_HUMAN	FBLN1	physical	21988832
GIT2_HUMAN	GIT2	physical	21988832
YTDC1_HUMAN	YTHDC1	physical	21988832
ABCF1_HUMAN	ABCF1	physical	22863883
NELFB_HUMAN	NELFB	physical	22863883
DDX1_HUMAN	DDX1	physical	22863883
DIM1_HUMAN	DIMT1	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
RFC4_HUMAN	RFC4	physical	22863883
DCP1A_HUMAN	DCP1A	physical	24778252
DCP2_HUMAN	DCP2	physical	24778252

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 EDC4_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6; SER-725; SER-844; SER-875; SER-879 ANDSER-887, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-676; THR-693; SER-725;SER-729; SER-741; SER-875; SER-879 AND SER-892, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-727;SER-729; SER-871; SER-875 AND SER-879, AND MASS SPECTROMETRY.	19369195 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6; SER-725; SER-844; SER-875; SER-879 ANDSER-887, AND MASS SPECTROMETRY.	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 THR-693; SER-725; SER-809;THR-821; SER-844 AND SER-879, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-723; SER-729;SER-780 AND SER-871, AND MASS SPECTROMETRY.	18691976 [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-723; SER-725; THR-727;SER-729 AND SER-734, AND MASS SPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-741, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 AND THR-1072, ANDMASS SPECTROMETRY.	16565220 [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-844, AND MASSSPECTROMETRY.	16964243 [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-729, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASSSPECTROMETRY.	17924679 [Abstract]