dbPTM

DDX41_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX41_HUMAN
UniProt AC	Q9UJV9
Protein Name	Probable ATP-dependent RNA helicase DDX41
Gene Name	DDX41
Organism	Homo sapiens (Human).
Sequence Length	622
Subcellular Localization	Nucleus .
Protein Description	Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing..
Protein Sequence	MEESEPERKRARTDEVPAGGSRSEAEDEDDEDYVPYVPLRQRRQLLLQKLLQRRRKGAAEEEQQDSGSEPRGDEDDIPLGPQSNVSLLDQHQHLKEKAEARKESAKEKQLKEEEKILESVAEGRALMSVKEMAKGITYDDPIKTSWTPPRYVLSMSEERHERVRKKYHILVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELARQTHGILEYYCRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEAKMVYLLECLQKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFINKACDESVLMDLKALLLEAKQKVPPVLQVLHCGDESMLDIGGERGCAFCGGLGHRITDCPKLEAMQTKQVSNIGRKDYLAHSSMDF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MEESEPERKRA ----CCCCHHHHHHC	45.18	29255136
9	Sumoylation	EESEPERKRARTDEV CCCHHHHHHCCCCCC	49.07	-
9	Sumoylation	EESEPERKRARTDEV CCCHHHHHHCCCCCC	49.07	-
13	Phosphorylation	PERKRARTDEVPAGG HHHHHCCCCCCCCCC	35.21	23927012
21	Phosphorylation	DEVPAGGSRSEAEDE CCCCCCCCCCCCCCC	31.54	29255136
23	Phosphorylation	VPAGGSRSEAEDEDD CCCCCCCCCCCCCCC	42.74	19664994
33	Phosphorylation	EDEDDEDYVPYVPLR CCCCCCCCCCCCCHH	10.98	23927012
36	Phosphorylation	DDEDYVPYVPLRQRR CCCCCCCCCCHHHHH	12.49	23927012
49	Ubiquitination	RRQLLLQKLLQRRRK HHHHHHHHHHHHHHC	51.65	21890473
56	Acetylation	KLLQRRRKGAAEEEQ HHHHHHHCCHHHHHH	51.60	26051181
66	Phosphorylation	AEEEQQDSGSEPRGD HHHHHHCCCCCCCCC	39.62	29255136
68	Phosphorylation	EEQQDSGSEPRGDED HHHHCCCCCCCCCCC	48.67	29255136
71	Methylation	QDSGSEPRGDEDDIP HCCCCCCCCCCCCCC	62.23	-
83	Phosphorylation	DIPLGPQSNVSLLDQ CCCCCCCCCCHHHHH	42.19	23927012
86	Phosphorylation	LGPQSNVSLLDQHQH CCCCCCCHHHHHHHH	27.71	23403867
95	Ubiquitination	LDQHQHLKEKAEARK HHHHHHHHHHHHHHH	55.85	-
111	Sumoylation	SAKEKQLKEEEKILE HHHHHHHHHHHHHHH	61.66	-
111	Sumoylation	SAKEKQLKEEEKILE HHHHHHHHHHHHHHH	61.66	-
115	Ubiquitination	KQLKEEEKILESVAE HHHHHHHHHHHHHHH	56.74	-
128	Phosphorylation	AEGRALMSVKEMAKG HHHHHHHCHHHHHCC	30.78	24719451
130	Acetylation	GRALMSVKEMAKGIT HHHHHCHHHHHCCCC	34.17	25953088
130	Ubiquitination	GRALMSVKEMAKGIT HHHHHCHHHHHCCCC	34.17	-
138	Phosphorylation	EMAKGITYDDPIKTS HHHCCCCCCCCCCCC	19.21	-
143	Ubiquitination	ITYDDPIKTSWTPPR CCCCCCCCCCCCCCC	41.72	-
145	Phosphorylation	YDDPIKTSWTPPRYV CCCCCCCCCCCCCEE	24.77	30631047
147	Phosphorylation	DPIKTSWTPPRYVLS CCCCCCCCCCCEEEC	24.15	21815630
154	Phosphorylation	TPPRYVLSMSEERHE CCCCEEECCCHHHHH	15.37	30631047
156	Phosphorylation	PRYVLSMSEERHERV CCEEECCCHHHHHHH	32.69	20860994
182	Phosphorylation	GIPPPIKSFKEMKFP CCCCCCCCHHHCCCH	42.12	24719451
194	Methylation	KFPAAILRGLKKKGI CCHHHHHHHHHHCCC	42.14	-
199	Ubiquitination	ILRGLKKKGIHHPTP HHHHHHHCCCCCCCC	62.60	-
232	Phosphorylation	AFTGSGKTLVFTLPV EECCCCCEEEEEHHH	31.51	24114839
236	Phosphorylation	SGKTLVFTLPVIMFC CCCEEEEEHHHHHHH	23.75	24114839
254	Ubiquitination	EKRLPFSKREGPYGL HCCCCCCCCCCCCEE	55.64	-
259	Phosphorylation	FSKREGPYGLIICPS CCCCCCCCEEEECCC	35.11	28152594
288	Phosphorylation	CRLLQEDSSPLLRCA HHHHHCCCCHHHHHH	32.86	27966365
289	Phosphorylation	RLLQEDSSPLLRCAL HHHHCCCCHHHHHHH	31.71	26699800
302	Phosphorylation	ALCIGGMSVKEQMET HHHHCCCCHHHHHHH	33.06	24719451
320	Phosphorylation	GVHMMVATPGRLMDL CCCEEECCHHHHHHH	18.18	23312004
330	Ubiquitination	RLMDLLQKKMVSLDI HHHHHHHHHCCCHHH	42.69	-
330	Acetylation	RLMDLLQKKMVSLDI HHHHHHHHHCCCHHH	42.69	25953088
331	Ubiquitination	LMDLLQKKMVSLDIC HHHHHHHHCCCHHHH	31.41	-
331	Acetylation	LMDLLQKKMVSLDIC HHHHHHHHCCCHHHH	31.41	27452117
364	Phosphorylation	DIRTIFSYFKGQRQT CHHHHHHHHCCCCEE	9.88	-
366	Methylation	RTIFSYFKGQRQTLL HHHHHHHCCCCEEEE	45.99	-
381	Ubiquitination	FSATMPKKIQNFAKS EECCCCHHHHHHHHH	43.59	-
388	Phosphorylation	KIQNFAKSALVKPVT HHHHHHHHHCCCCEE	24.33	20860994
392	Sumoylation	FAKSALVKPVTINVG HHHHHCCCCEEEECC	34.32	-
392	Sumoylation	FAKSALVKPVTINVG HHHHHCCCCEEEECC	34.32	-
392	Ubiquitination	FAKSALVKPVTINVG HHHHHCCCCEEEECC	34.32	-
395	Phosphorylation	SALVKPVTINVGRAG HHCCCCEEEECCCCC	18.50	-
405	Phosphorylation	VGRAGAASLDVIQEV CCCCCCCCCHHHHHH	25.27	28348404
414	Phosphorylation	DVIQEVEYVKEEAKM HHHHHHHHHHHHHHH	23.23	-
416	Ubiquitination	IQEVEYVKEEAKMVY HHHHHHHHHHHHHHH	49.27	-
416	Sumoylation	IQEVEYVKEEAKMVY HHHHHHHHHHHHHHH	49.27	-
416	Sumoylation	IQEVEYVKEEAKMVY HHHHHHHHHHHHHHH	49.27	28112733
416	Acetylation	IQEVEYVKEEAKMVY HHHHHHHHHHHHHHH	49.27	25953088
441	2-Hydroxyisobutyrylation	PVLIFAEKKADVDAI CEEEEECCCCCHHHH	50.24	-
442	Ubiquitination	VLIFAEKKADVDAIH EEEEECCCCCHHHHH	41.13	-
442	Sumoylation	VLIFAEKKADVDAIH EEEEECCCCCHHHHH	41.13	-
442	Sumoylation	VLIFAEKKADVDAIH EEEEECCCCCHHHHH	41.13	28112733
455	Ubiquitination	IHEYLLLKGVEAVAI HHHHHHHHCCEEEEE	61.96	-
466	Ubiquitination	AVAIHGGKDQEERTK EEEECCCCCHHHHHH	61.91	-
473	Ubiquitination	KDQEERTKAIEAFRE CCHHHHHHHHHHHHH	54.29	-
482	Ubiquitination	IEAFREGKKDVLVAT HHHHHHCCCCEEEEE	40.84	-
493	Phosphorylation	LVATDVASKGLDFPA EEEEHHHCCCCCCCH	27.40	24114839
523	Phosphorylation	YVHRIGRTGRSGNTG HHHHHCCCCCCCCCC	31.56	20068231
526	Phosphorylation	RIGRTGRSGNTGIAT HHCCCCCCCCCCEEH	37.43	20068231
529	Phosphorylation	RTGRSGNTGIATTFI CCCCCCCCCEEHHHH	33.23	28509920
533	Phosphorylation	SGNTGIATTFINKAC CCCCCEEHHHHHHHC	21.96	20068231
534	Phosphorylation	GNTGIATTFINKACD CCCCEEHHHHHHHCC	17.31	28509920
538	Ubiquitination	IATTFINKACDESVL EEHHHHHHHCCHHHH	45.64	-
549	Ubiquitination	ESVLMDLKALLLEAK HHHHHHHHHHHHHHH	32.49	-
556	Ubiquitination	KALLLEAKQKVPPVL HHHHHHHHHHCCCEE	41.08	-
572	Phosphorylation	VLHCGDESMLDIGGE EEEECCHHHCCCCCC	29.41	30576142
597	Ubiquitination	HRITDCPKLEAMQTK CCCCCCHHHHHHHCC	66.35	-
603	Phosphorylation	PKLEAMQTKQVSNIG HHHHHHHCCCCCCCC	15.45	22673903
604	Ubiquitination	KLEAMQTKQVSNIGR HHHHHHCCCCCCCCC	31.63	-
612	Ubiquitination	QVSNIGRKDYLAHSS CCCCCCCCHHHHHCC	45.58	-
614	Phosphorylation	SNIGRKDYLAHSSMD CCCCCCHHHHHCCCC	14.60	26270265
618	Phosphorylation	RKDYLAHSSMDF--- CCHHHHHCCCCC---	23.04	25159151
619	Phosphorylation	KDYLAHSSMDF---- CHHHHHCCCCC----	16.71	25159151

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
414	Y	Phosphorylation	Kinase	BTK	Q06187	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDX41_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 DDX41_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NKAP_HUMAN	NKAP	physical	22365833
CEP70_HUMAN	CEP70	physical	25416956
CLVS2_HUMAN	CLVS2	physical	26344197
PREP_HUMAN	PITRM1	physical	26344197
ANR50_HUMAN	ANKRD50	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
PININ_HUMAN	PNN	physical	28514442
SIN3A_HUMAN	SIN3A	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
BRM1L_HUMAN	BRMS1L	physical	28514442
CBY1_HUMAN	CBY1	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 DDX41_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-21 AND SER-23, 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-21 AND SER-23, 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-21 AND SER-23, 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-23, AND MASSSPECTROMETRY.	18220336 [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-23, AND MASSSPECTROMETRY.	16565220 [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-21 AND SER-23, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-23, AND MASSSPECTROMETRY.	15302935 [Abstract]