dbPTM

DDX5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX5_HUMAN
UniProt AC	P17844
Protein Name	Probable ATP-dependent RNA helicase DDX5
Gene Name	DDX5
Organism	Homo sapiens (Human).
Sequence Length	614
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms..
Protein Sequence	MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGYSSDRD ------CCCCCCCCC	46.57	23401153
4	Phosphorylation	----MSGYSSDRDRG ----CCCCCCCCCCC	9.55	20873877
5	Phosphorylation	---MSGYSSDRDRGR ---CCCCCCCCCCCC	29.32	23401153
6	Phosphorylation	--MSGYSSDRDRGRD --CCCCCCCCCCCCC	28.34	23401153
10	Methylation	GYSSDRDRGRDRGFG CCCCCCCCCCCCCCC	42.83	-
12	Methylation	SSDRDRGRDRGFGAP CCCCCCCCCCCCCCC	31.20	-
14	Methylation	DRDRGRDRGFGAPRF CCCCCCCCCCCCCCC	40.76	-
20	Methylation	DRGFGAPRFGGSRAG CCCCCCCCCCCCCCC	42.16	-
24	Phosphorylation	GAPRFGGSRAGPLSG CCCCCCCCCCCCCCC	21.24	25159151
25	Methylation	APRFGGSRAGPLSGK CCCCCCCCCCCCCCC	47.00	-
30	Phosphorylation	GSRAGPLSGKKFGNP CCCCCCCCCCCCCCC	52.26	21712546
32	Acetylation	RAGPLSGKKFGNPGE CCCCCCCCCCCCCCH	41.37	-
32	Acetylation	RAGPLSGKKFGNPGE CCCCCCCCCCCCCCH	41.37	19608861
32	Sumoylation	RAGPLSGKKFGNPGE CCCCCCCCCCCCCCH	41.37	28112733
32	Ubiquitination	RAGPLSGKKFGNPGE CCCCCCCCCCCCCCH	41.37	19608861
33	Acetylation	AGPLSGKKFGNPGEK CCCCCCCCCCCCCHH	63.13	19608861
33	Ubiquitination	AGPLSGKKFGNPGEK CCCCCCCCCCCCCHH	63.13	19608861
40	Acetylation	KFGNPGEKLVKKKWN CCCCCCHHHHHHCCC	65.58	-
40	Ubiquitination	KFGNPGEKLVKKKWN CCCCCCHHHHHHCCC	65.58	-
40	Acetylation	KFGNPGEKLVKKKWN CCCCCCHHHHHHCCC	65.58	19608861
40	Sumoylation	KFGNPGEKLVKKKWN CCCCCCHHHHHHCCC	65.58	19608861
40	Ubiquitination	KFGNPGEKLVKKKWN CCCCCCHHHHHHCCC	65.58	19608861
43	Acetylation	NPGEKLVKKKWNLDE CCCHHHHHHCCCHHH	60.10	20663877
44	Acetylation	PGEKLVKKKWNLDEL CCHHHHHHCCCHHHC	56.39	20663877
45	Sumoylation	GEKLVKKKWNLDELP CHHHHHHCCCHHHCC	35.28	-
45	Acetylation	GEKLVKKKWNLDELP CHHHHHHCCCHHHCC	35.28	20663877
45	Sumoylation	GEKLVKKKWNLDELP CHHHHHHCCCHHHCC	35.28	28112733
45	Ubiquitination	GEKLVKKKWNLDELP CHHHHHHCCCHHHCC	35.28	-
53	Ubiquitination	WNLDELPKFEKNFYQ CCHHHCCHHHHHHHH	77.95	-
53	Sumoylation	WNLDELPKFEKNFYQ CCHHHCCHHHHHHHH	77.95	-
53	Acetylation	WNLDELPKFEKNFYQ CCHHHCCHHHHHHHH	77.95	25953088
53	Sumoylation	WNLDELPKFEKNFYQ CCHHHCCHHHHHHHH	77.95	25114211
53	Ubiquitination	WNLDELPKFEKNFYQ CCHHHCCHHHHHHHH	77.95	21906983
56	Methylation	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	-
56	Ubiquitination	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	21890473
56	Sumoylation	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	-
56	Acetylation	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	20663877
56	Methylation	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	23644510
56	Sumoylation	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	-
56	Ubiquitination	DELPKFEKNFYQEHP HHCCHHHHHHHHHCH	56.33	21890473
59	Phosphorylation	PKFEKNFYQEHPDLA CHHHHHHHHHCHHHH	23.53	28152594
75	Phosphorylation	RTAQEVETYRRSKEI HHHHHHHHHHHHCCE	27.75	28152594
76	Phosphorylation	TAQEVETYRRSKEIT HHHHHHHHHHHCCEE	7.19	28152594
79	O-linked_Glycosylation	EVETYRRSKEITVRG HHHHHHHHCCEEECC	26.16	28510447
79	Phosphorylation	EVETYRRSKEITVRG HHHHHHHHCCEEECC	26.16	28634120
80	Ubiquitination	VETYRRSKEITVRGH HHHHHHHCCEEECCC	51.85	-
80	Acetylation	VETYRRSKEITVRGH HHHHHHHCCEEECCC	51.85	20663877
80	Ubiquitination	VETYRRSKEITVRGH HHHHHHHCCEEECCC	51.85	21906983
83	Phosphorylation	YRRSKEITVRGHNCP HHHHCCEEECCCCCC	12.77	-
91	Acetylation	VRGHNCPKPVLNFYE ECCCCCCCCCCCHHH	50.38	26051181
91	Ubiquitination	VRGHNCPKPVLNFYE ECCCCCCCCCCCHHH	50.38	-
97	Phosphorylation	PKPVLNFYEANFPAN CCCCCCHHHCCCCHH	17.04	-
118	Ubiquitination	RQNFTEPTAIQAQGW HCCCCCCCCHHHCCC	30.11	-
128	Ubiquitination	QAQGWPVALSGLDMV HHCCCCEEECCEEEE	7.60	-
144	Ubiquitination	VAQTGSGKTLSYLLP EEECCCCHHHHHHHH	48.25	-
157	Acetylation	LPAIVHINHQPFLER HHEEHEECCHHHHCC	16.92	-
157	Ubiquitination	LPAIVHINHQPFLER HHEEHEECCHHHHCC	16.92	-
170	Glutathionylation	ERGDGPICLVLAPTR CCCCCCEEEEEECHH	2.12	22555962
185	Acetylation	ELAQQVQQVAAEYCR HHHHHHHHHHHHHHH	28.14	-
185	Ubiquitination	ELAQQVQQVAAEYCR HHHHHHHHHHHHHHH	28.14	-
190	Phosphorylation	VQQVAAEYCRACRLK HHHHHHHHHHHHCCC	5.19	28152594
191	Glutathionylation	QQVAAEYCRACRLKS HHHHHHHHHHHCCCC	1.35	22555962
191	S-palmitoylation	QQVAAEYCRACRLKS HHHHHHHHHHHCCCC	1.35	26865113
197	Acetylation	YCRACRLKSTCIYGG HHHHHCCCCEEEECC	25.11	26051181
197	Methylation	YCRACRLKSTCIYGG HHHHHCCCCEEEECC	25.11	-
197	Ubiquitination	YCRACRLKSTCIYGG HHHHHCCCCEEEECC	25.11	21890473
198	Phosphorylation	CRACRLKSTCIYGGA HHHHCCCCEEEECCC	32.86	28152594
199	Phosphorylation	RACRLKSTCIYGGAP HHHCCCCEEEECCCC	11.01	28152594
200	S-nitrosocysteine	ACRLKSTCIYGGAPK HHCCCCEEEECCCCC	2.66	-
200	Glutathionylation	ACRLKSTCIYGGAPK HHCCCCEEEECCCCC	2.66	22555962
200	S-nitrosylation	ACRLKSTCIYGGAPK HHCCCCEEEECCCCC	2.66	19483679
202	Phosphorylation	RLKSTCIYGGAPKGP CCCCEEEECCCCCCC	16.20	27273156
205	Ubiquitination	STCIYGGAPKGPQIR CEEEECCCCCCCCCC	9.77	-
207	Acetylation	CIYGGAPKGPQIRDL EEECCCCCCCCCCCH	80.72	26051181
207	Malonylation	CIYGGAPKGPQIRDL EEECCCCCCCCCCCH	80.72	26320211
207	Sumoylation	CIYGGAPKGPQIRDL EEECCCCCCCCCCCH	80.72	-
207	Ubiquitination	CIYGGAPKGPQIRDL EEECCCCCCCCCCCH	80.72	-
214	Ubiquitination	KGPQIRDLERGVEIC CCCCCCCHHCCEEEE	3.29	21890473
221	Glutathionylation	LERGVEICIATPGRL HHCCEEEEEECCCCE	0.80	22555962
221	S-palmitoylation	LERGVEICIATPGRL HHCCEEEEEECCCCE	0.80	29575903
224	Phosphorylation	GVEICIATPGRLIDF CEEEEEECCCCEEEH	13.33	30266825
234	S-nitrosocysteine	RLIDFLECGKTNLRR CEEEHHHCCCCCCCC	8.03	-
234	Glutathionylation	RLIDFLECGKTNLRR CEEEHHHCCCCCCCC	8.03	22555962
234	S-nitrosylation	RLIDFLECGKTNLRR CEEEHHHCCCCCCCC	8.03	19483679
236	Acetylation	IDFLECGKTNLRRTT EEHHHCCCCCCCCEE	45.99	23954790
236	Ubiquitination	IDFLECGKTNLRRTT EEHHHCCCCCCCCEE	45.99	21906983
242	Phosphorylation	GKTNLRRTTYLVLDE CCCCCCCEEEEEEEH	17.23	28152594
243	Phosphorylation	KTNLRRTTYLVLDEA CCCCCCEEEEEEEHH	17.04	28152594
244	Phosphorylation	TNLRRTTYLVLDEAD CCCCCEEEEEEEHHH	8.32	28152594
261	Acetylation	LDMGFEPQIRKIVDQ HHCCCHHHHHHHHHH	40.70	-
261	Ubiquitination	LDMGFEPQIRKIVDQ HHCCCHHHHHHHHHH	40.70	-
263	Methylation	MGFEPQIRKIVDQIR CCCHHHHHHHHHHHC	19.87	-
264	Ubiquitination	GFEPQIRKIVDQIRP CCHHHHHHHHHHHCC	49.03	-
264	Acetylation	GFEPQIRKIVDQIRP CCHHHHHHHHHHHCC	49.03	23749302
264	Malonylation	GFEPQIRKIVDQIRP CCHHHHHHHHHHHCC	49.03	26320211
264	Ubiquitination	GFEPQIRKIVDQIRP CCHHHHHHHHHHHCC	49.03	-
272	Ubiquitination	IVDQIRPDRQTLMWS HHHHHCCCCCEEEEE	45.53	-
273	Methylation	VDQIRPDRQTLMWSA HHHHCCCCCEEEEEC	33.78	-
279	Phosphorylation	DRQTLMWSATWPKEV CCCEEEEECCCCHHH	11.23	-
284	Acetylation	MWSATWPKEVRQLAE EEECCCCHHHHHHHH	61.47	26051181
284	Ubiquitination	MWSATWPKEVRQLAE EEECCCCHHHHHHHH	61.47	21906983
296	Ubiquitination	LAEDFLKDYIHINIG HHHHHHHHCCEEECC	50.17	-
297	Phosphorylation	AEDFLKDYIHINIGA HHHHHHHCCEEECCC	7.88	22817900
309	Ubiquitination	IGALELSANHNILQI CCCEEHHCCCCEEEH	33.65	-
312	Ubiquitination	LELSANHNILQIVDV EEHHCCCCEEEHHHH	36.15	-
318	Ubiquitination	HNILQIVDVCHDVEK CCEEEHHHHHCCCHH	38.67	21890473
328	Ubiquitination	HDVEKDEKLIRLMEE CCCHHCHHHHHHHHH	60.39	-
332	Ubiquitination	KDEKLIRLMEEIMSE HCHHHHHHHHHHHCC	3.93	-
333	Sulfoxidation	DEKLIRLMEEIMSEK CHHHHHHHHHHHCCC	2.89	21406390
338	Phosphorylation	RLMEEIMSEKENKTI HHHHHHHCCCCCCEE	51.70	20068231
340	Acetylation	MEEIMSEKENKTIVF HHHHHCCCCCCEEEE	60.32	23749302
340	Methylation	MEEIMSEKENKTIVF HHHHHCCCCCCEEEE	60.32	-
340	Sumoylation	MEEIMSEKENKTIVF HHHHHCCCCCCEEEE	60.32	28112733
340	Ubiquitination	MEEIMSEKENKTIVF HHHHHCCCCCCEEEE	60.32	21906983
343	Sumoylation	IMSEKENKTIVFVET HHCCCCCCEEEEEEC	40.49	28112733
343	Ubiquitination	IMSEKENKTIVFVET HHCCCCCCEEEEEEC	40.49	-
344	Phosphorylation	MSEKENKTIVFVETK HCCCCCCEEEEEECH	33.67	21406692
350	Phosphorylation	KTIVFVETKRRCDEL CEEEEEECHHHHHHH	25.25	21406692
351	Acetylation	TIVFVETKRRCDELT EEEEEECHHHHHHHH	25.08	25953088
351	Ubiquitination	TIVFVETKRRCDELT EEEEEECHHHHHHHH	25.08	21906983
358	Ubiquitination	KRRCDELTRKMRRDG HHHHHHHHHHHHHCC	26.62	-
367	Ubiquitination	KMRRDGWPAMGIHGD HHHHCCCCCCCCCCC	20.21	21890473
372	Ubiquitination	GWPAMGIHGDKSQQE CCCCCCCCCCHHHHH	32.44	-
375	Ubiquitination	AMGIHGDKSQQERDW CCCCCCCHHHHHHHH	55.55	21906983
376	Phosphorylation	MGIHGDKSQQERDWV CCCCCCHHHHHHHHH	41.66	20873877
388	Acetylation	DWVLNEFKHGKAPIL HHHHHHHHCCCCCEE	45.31	25825284
388	Sumoylation	DWVLNEFKHGKAPIL HHHHHHHHCCCCCEE	45.31	28112733
388	Ubiquitination	DWVLNEFKHGKAPIL HHHHHHHHCCCCCEE	45.31	21890473
391	Acetylation	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	-
391	Ubiquitination	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	-
391	Sumoylation	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	-
391	Acetylation	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	25953088
391	Malonylation	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	33225896
391	Sumoylation	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	28112733
391	Ubiquitination	LNEFKHGKAPILIAT HHHHHCCCCCEEEEE	51.19	21906983
398	Phosphorylation	KAPILIATDVASRGL CCCEEEEECHHHCCC	24.82	29255136
400	Ubiquitination	PILIATDVASRGLDV CEEEEECHHHCCCCH	4.53	21890473
402	Phosphorylation	LIATDVASRGLDVED EEEECHHHCCCCHHH	27.08	29255136
403	Methylation	IATDVASRGLDVEDV EEECHHHCCCCHHHE	39.70	-
411	Sumoylation	GLDVEDVKFVINYDY CCCHHHEEEEEECCC	46.35	-
411	Acetylation	GLDVEDVKFVINYDY CCCHHHEEEEEECCC	46.35	26051181
411	Sumoylation	GLDVEDVKFVINYDY CCCHHHEEEEEECCC	46.35	28112733
411	Ubiquitination	GLDVEDVKFVINYDY CCCHHHEEEEEECCC	46.35	21906983
416	Phosphorylation	DVKFVINYDYPNSSE HEEEEEECCCCCCCH	13.01	28796482
418	Phosphorylation	KFVINYDYPNSSEDY EEEEECCCCCCCHHH	8.24	28796482
421	Phosphorylation	INYDYPNSSEDYIHR EECCCCCCCHHHHHH	30.51	28152594
422	Phosphorylation	NYDYPNSSEDYIHRI ECCCCCCCHHHHHHH	40.92	28152594
425	Phosphorylation	YPNSSEDYIHRIGRT CCCCCHHHHHHHHCC	8.45	28152594
437	Sumoylation	GRTARSTKTGTAYTF HCCCCCCCCCCEEEE	46.32	-
437	Acetylation	GRTARSTKTGTAYTF HCCCCCCCCCCEEEE	46.32	25953088
437	Sumoylation	GRTARSTKTGTAYTF HCCCCCCCCCCEEEE	46.32	28112733
437	Ubiquitination	GRTARSTKTGTAYTF HCCCCCCCCCCEEEE	46.32	21890473
438	Phosphorylation	RTARSTKTGTAYTFF CCCCCCCCCCEEEEE	39.59	28152594
440	Phosphorylation	ARSTKTGTAYTFFTP CCCCCCCCEEEEECC	23.02	28152594
442	Phosphorylation	STKTGTAYTFFTPNN CCCCCCEEEEECCCC	12.15	20090780
443	Phosphorylation	TKTGTAYTFFTPNNI CCCCCEEEEECCCCH	15.14	29396449
444	Ubiquitination	KTGTAYTFFTPNNIK CCCCEEEEECCCCHH	4.12	-
446	Phosphorylation	GTAYTFFTPNNIKQV CCEEEEECCCCHHHH	22.40	25159151
451	Sumoylation	FFTPNNIKQVSDLIS EECCCCHHHHHHHHH	46.93	28112733
451	Ubiquitination	FFTPNNIKQVSDLIS EECCCCHHHHHHHHH	46.93	21906983
453	Ubiquitination	TPNNIKQVSDLISVL CCCCHHHHHHHHHHH	4.00	21890473
454	Phosphorylation	PNNIKQVSDLISVLR CCCHHHHHHHHHHHH	24.97	30266825
458	Phosphorylation	KQVSDLISVLREANQ HHHHHHHHHHHHHHH	23.54	30266825
470	Sumoylation	ANQAINPKLLQLVED HHHHHCHHHHHHHHH	58.29	-
470	Acetylation	ANQAINPKLLQLVED HHHHHCHHHHHHHHH	58.29	23236377
470	Sumoylation	ANQAINPKLLQLVED HHHHHCHHHHHHHHH	58.29	28112733
470	Ubiquitination	ANQAINPKLLQLVED HHHHHCHHHHHHHHH	58.29	21890473
478	Methylation	LLQLVEDRGSGRSRG HHHHHHHCCCCCCCC	27.89	-
480	Phosphorylation	QLVEDRGSGRSRGRG HHHHHCCCCCCCCCC	31.74	25159151
483	Phosphorylation	EDRGSGRSRGRGGMK HHCCCCCCCCCCCCC	42.48	27067055
484	Dimethylation	DRGSGRSRGRGGMKD HCCCCCCCCCCCCCC	37.15	-
484	Methylation	DRGSGRSRGRGGMKD HCCCCCCCCCCCCCC	37.15	-
486	Dimethylation	GSGRSRGRGGMKDDR CCCCCCCCCCCCCCC	37.06	-
486	Methylation	GSGRSRGRGGMKDDR CCCCCCCCCCCCCCC	37.06	-
490	Methylation	SRGRGGMKDDRRDRY CCCCCCCCCCCCHHH	60.80	-
497	Phosphorylation	KDDRRDRYSAGKRGG CCCCCHHHCCCCCCC	13.73	28102081
498	Phosphorylation	DDRRDRYSAGKRGGF CCCCHHHCCCCCCCC	31.29	20068231
501	Acetylation	RDRYSAGKRGGFNTF CHHHCCCCCCCCCCC	47.81	7378523
502	Dimethylation	DRYSAGKRGGFNTFR HHHCCCCCCCCCCCC	49.93	-
502	Methylation	DRYSAGKRGGFNTFR HHHCCCCCCCCCCCC	49.93	15782174
507	Phosphorylation	GKRGGFNTFRDRENY CCCCCCCCCCCCCCC	20.13	18212344
509	Methylation	RGGFNTFRDRENYDR CCCCCCCCCCCCCHH	39.78	-
514	Phosphorylation	TFRDRENYDRGYSSL CCCCCCCCHHCHHHH	11.41	23917254
516	Methylation	RDRENYDRGYSSLLK CCCCCCHHCHHHHHH	35.27	-
518	Phosphorylation	RENYDRGYSSLLKRD CCCCHHCHHHHHHHH	8.93	28555341
519	Phosphorylation	ENYDRGYSSLLKRDF CCCHHCHHHHHHHHC	19.82	21712546
520	Phosphorylation	NYDRGYSSLLKRDFG CCHHCHHHHHHHHCC	29.27	23401153
523	Sumoylation	RGYSSLLKRDFGAKT HCHHHHHHHHCCCCC	56.04	-
523	Acetylation	RGYSSLLKRDFGAKT HCHHHHHHHHCCCCC	56.04	25953088
523	Sumoylation	RGYSSLLKRDFGAKT HCHHHHHHHHCCCCC	56.04	28112733
523	Ubiquitination	RGYSSLLKRDFGAKT HCHHHHHHHHCCCCC	56.04	21890473
535	Phosphorylation	AKTQNGVYSAANYTN CCCCCCEEEECCCCC	8.26	-
536	O-linked_Glycosylation	KTQNGVYSAANYTNG CCCCCEEEECCCCCC	20.64	28510447
544	O-linked_Glycosylation	AANYTNGSFGSNFVS ECCCCCCCCCCCCEE	28.62	28510447
551	O-linked_Glycosylation	SFGSNFVSAGIQTSF CCCCCCEECEEEEEE	19.35	28510447
551	Phosphorylation	SFGSNFVSAGIQTSF CCCCCCEECEEEEEE	19.35	21601212
557	O-linked_Glycosylation	VSAGIQTSFRTGNPT EECEEEEEECCCCCC	9.06	28510447
557	Phosphorylation	VSAGIQTSFRTGNPT EECEEEEEECCCCCC	9.06	7525583
564	Phosphorylation	SFRTGNPTGTYQNGY EECCCCCCCCCCCCC	46.27	-
593	Phosphorylation	NGMNQQAYAYPATAA CCCCCCCCCCCCCCC	11.43	22817900
595	Phosphorylation	MNQQAYAYPATAAAP CCCCCCCCCCCCCCC	4.82	22817900

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
198	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
446	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
557	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
557	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
564	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
593	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:16055720

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
502	R	Methylation		-
Arg-502 is dimethylated, probably to asymmetric dimethylarginine.

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 DDX5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_HUMAN	HDAC1	physical	15298701
CBP_HUMAN	CREBBP	physical	12527917
EP300_HUMAN	EP300	physical	12527917
AKAP8_HUMAN	AKAP8	physical	11279182
FBRL_HUMAN	FBL	physical	10837141
IPO11_HUMAN	IPO11	physical	17643375
AIRE_HUMAN	AIRE	physical	20085707
HDAC1_HUMAN	HDAC1	physical	20022962
SMCA4_HUMAN	SMARCA4	physical	17011493
TBP_HUMAN	TBP	physical	17011493
RPB1_HUMAN	POLR2A	physical	17011493
HDAC1_HUMAN	HDAC1	physical	17369852
ESR1_HUMAN	ESR1	physical	19995069
EP300_HUMAN	EP300	physical	19995069
DDX5_HUMAN	DDX5	physical	19995069
DDX17_HUMAN	DDX17	physical	19995069
HDAC1_HUMAN	HDAC1	physical	19995069
HDAC2_HUMAN	HDAC2	physical	19995069
HDAC3_HUMAN	HDAC3	physical	19995069
DHX15_HUMAN	DHX15	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
SF3B3_HUMAN	SF3B3	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
PRP16_HUMAN	DHX38	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
IF4A3_HUMAN	EIF4A3	physical	22939629
PRKDC_HUMAN	PRKDC	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
HNRPM_HUMAN	HNRNPM	physical	22939629
HNRPF_HUMAN	HNRNPF	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
RBMX_HUMAN	RBMX	physical	22939629
HNRPQ_HUMAN	SYNCRIP	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
PR40A_HUMAN	PRPF40A	physical	22939629
IF2B3_HUMAN	IGF2BP3	physical	22939629
SNW1_HUMAN	SNW1	physical	22939629
PRP19_HUMAN	PRPF19	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
MCM7_HUMAN	MCM7	physical	22939629
SYN1_HUMAN	SYN1	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
XRCC4_HUMAN	XRCC4	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
EF2_HUMAN	EEF2	physical	22939629
TRY1_HUMAN	PRSS1	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
GOLI4_HUMAN	GOLIM4	physical	22939629
SYEP_HUMAN	EPRS	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
SRP14_HUMAN	SRP14	physical	22939629
RBM10_HUMAN	RBM10	physical	22365833
ROA0_HUMAN	HNRNPA0	physical	22365833
WBP11_HUMAN	WBP11	physical	22365833
DDX17_HUMAN	DDX17	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
DHX9_HUMAN	DHX9	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
HNRH1_HUMAN	HNRNPH1	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
DDX17_HUMAN	DDX17	physical	22863883
LRSM1_HUMAN	LRSAM1	physical	22863883
PABP4_HUMAN	PABPC4	physical	22863883
KPRA_HUMAN	PRPSAP1	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
MAPK2_HUMAN	MAPKAPK2	physical	23482664
RNC_HUMAN	DROSHA	physical	23482664
EP300_HUMAN	EP300	physical	20663877
ESR1_HUMAN	ESR1	physical	20663877
ATX2_HUMAN	ATXN2	physical	26344197
ATX2L_HUMAN	ATXN2L	physical	26344197
CN166_HUMAN	C14orf166	physical	26344197
CPSF6_HUMAN	CPSF6	physical	26344197
DHX36_HUMAN	DHX36	physical	26344197
DHX9_HUMAN	DHX9	physical	26344197
EDC4_HUMAN	EDC4	physical	26344197
EIF2A_HUMAN	EIF2A	physical	26344197
IF4A3_HUMAN	EIF4A3	physical	26344197
GUAA_HUMAN	GMPS	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197
HNRH1_HUMAN	HNRNPH1	physical	26344197
IF2B3_HUMAN	IGF2BP3	physical	26344197
LC7L2_HUMAN	LUC7L2	physical	26344197
NACAM_HUMAN	NACA	physical	26344197
NACA_HUMAN	NACA	physical	26344197
SRRM1_HUMAN	SRRM1	physical	26344197
RENT1_HUMAN	UPF1	physical	26344197
RING2_HUMAN	RNF2	physical	28111200
CBX7_HUMAN	CBX7	physical	28111200
RYBP_HUMAN	RYBP	physical	28111200
YPEL5_HUMAN	YPEL5	physical	27173435
RANB9_HUMAN	RANBP9	physical	27173435
ARMC8_HUMAN	ARMC8	physical	27173435
SUZ12_HUMAN	SUZ12	physical	27338022

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 DDX5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-32; LYS-33 AND LYS-40, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-502, AND MASS SPECTROMETRY.	15782174 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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-480, AND MASSSPECTROMETRY.	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 SER-480, AND MASSSPECTROMETRY.	18691976 [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 THR-507 AND SER-520, ANDMASS SPECTROMETRY.	17287340 [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 SER-30, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-202, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, AND MASSSPECTROMETRY.	15592455 [Abstract]
Sumoylation
Reference	PubMed
"Sumoylation of p68 and p72 RNA helicases affects protein stabilityand transactivation potential."; Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.; Biochemistry 49:1-10(2010). Cited for: SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, AND POLYUBIQUITINATION.	19995069 [Abstract]
"SUMO modification of the DEAD box protein p68 modulates itstranscriptional activity and promotes its interaction with HDAC1."; Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T.,Fuller-Pace F.V.; Oncogene 26:5866-5876(2007). Cited for: SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, ANDMUTAGENESIS OF LYS-53 AND GLU-55.	17369852 [Abstract]

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