dbPTM

DHX15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHX15_HUMAN
UniProt AC	O43143
Protein Name	Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15
Gene Name	DHX15
Organism	Homo sapiens (Human).
Sequence Length	795
Subcellular Localization	Nucleus. Nucleus, nucleolus.
Protein Description	Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns..
Protein Sequence	MSKRHRLDLGEDYPSGKKRAGTDGKDRDRDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHAGHAGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSKRHRLDL ------CCCCCCCCC	38.10	26074081
3	Acetylation	-----MSKRHRLDLG -----CCCCCCCCCC	51.42	19813087
13	Phosphorylation	RLDLGEDYPSGKKRA CCCCCCCCCCCCCCC	8.59	27273156
15	Phosphorylation	DLGEDYPSGKKRAGT CCCCCCCCCCCCCCC	57.95	25159151
17	Acetylation	GEDYPSGKKRAGTDG CCCCCCCCCCCCCCC	43.34	23954790
17	Ubiquitination	GEDYPSGKKRAGTDG CCCCCCCCCCCCCCC	43.34	21906983
18	Acetylation	EDYPSGKKRAGTDGK CCCCCCCCCCCCCCC	51.51	7296667
18	Methylation	EDYPSGKKRAGTDGK CCCCCCCCCCCCCCC	51.51	23748837
18	Ubiquitination	EDYPSGKKRAGTDGK CCCCCCCCCCCCCCC	51.51	22817900
37	Phosphorylation	DRDREDRSKDRDRER CCCHHHHHHHHHHHH	51.75	30576142
42	Dimethylation	DRSKDRDRERDRGDR HHHHHHHHHHHHHHH	41.57	-
44	Dimethylation	SKDRDRERDRGDRER HHHHHHHHHHHHHHH	39.56	-
64	O-linked_Glycosylation	KEKELRASTNAMLIS HHHHHHHHHHHHHHH	18.76	23301498
64	Phosphorylation	KEKELRASTNAMLIS HHHHHHHHHHHHHHH	18.76	28555341
65	Phosphorylation	EKELRASTNAMLISA HHHHHHHHHHHHHHC	26.47	25159151
68	Sulfoxidation	LRASTNAMLISAGLP HHHHHHHHHHHCCCC	3.56	21406390
71	Phosphorylation	STNAMLISAGLPPLK HHHHHHHHCCCCCCC	16.60	27251275
128	Phosphorylation	LPHTPRYYDILKKRL CCCCHHHHHHHHHHC	9.59	-
132	Acetylation	PRYYDILKKRLQLPV HHHHHHHHHHCCCCC	35.86	23749302
132	Ubiquitination	PRYYDILKKRLQLPV HHHHHHHHHHCCCCC	35.86	21906983
133	Ubiquitination	RYYDILKKRLQLPVW HHHHHHHHHCCCCCE	55.70	22817900
142	Phosphorylation	LQLPVWEYKDRFTDI CCCCCEEEHHHHHHH	11.50	28152594
143	Acetylation	QLPVWEYKDRFTDIL CCCCEEEHHHHHHHE	30.80	25953088
143	Ubiquitination	QLPVWEYKDRFTDIL CCCCEEEHHHHHHHE	30.80	21963094
155	Phosphorylation	DILVRHQSFVLVGET HHEEECCEEEEEECC	15.93	20873877
162	Phosphorylation	SFVLVGETGSGKTTQ EEEEEECCCCCCCCC	30.62	21406692
164	Phosphorylation	VLVGETGSGKTTQIP EEEECCCCCCCCCCC	44.53	21406692
166	Acetylation	VGETGSGKTTQIPQW EECCCCCCCCCCCHH	50.53	20167786
166	Ubiquitination	VGETGSGKTTQIPQW EECCCCCCCCCCCHH	50.53	21963094
167	O-linked_Glycosylation	GETGSGKTTQIPQWC ECCCCCCCCCCCHHH	27.71	23301498
174	Glutathionylation	TTQIPQWCVEYMRSL CCCCCHHHHHHHHCC	1.08	22555962
185	Acetylation	MRSLPGPKRGVACTQ HHCCCCCCCCCCCCC	68.64	20167786
190	S-nitrosocysteine	GPKRGVACTQPRRVA CCCCCCCCCCHHHHH	3.18	-
190	S-nitrosylation	GPKRGVACTQPRRVA CCCCCCCCCCHHHHH	3.18	19483679
200	Phosphorylation	PRRVAAMSVAQRVAD HHHHHHHHHHHHHHH	15.01	30242111
219	Phosphorylation	MLGQEVGYSIRFEDC HHCCCCCCEEEECCC	13.19	20068231
220	Phosphorylation	LGQEVGYSIRFEDCS HCCCCCCEEEECCCC	11.02	24719451
230	Acetylation	FEDCSSAKTILKYMT ECCCCCCHHHHHHHH	37.74	25953088
230	Ubiquitination	FEDCSSAKTILKYMT ECCCCCCHHHHHHHH	37.74	27667366
234	Acetylation	SSAKTILKYMTDGML CCCHHHHHHHHHHHH	29.17	26051181
234	Ubiquitination	SSAKTILKYMTDGML CCCHHHHHHHHHHHH	29.17	21906983
246	Sulfoxidation	GMLLREAMNDPLLER HHHHHHHHCCHHHHH	5.11	21406390
254	Phosphorylation	NDPLLERYGVIILDE CCHHHHHHCEEEECH	13.33	28152594
266	Phosphorylation	LDEAHERTLATDILM ECHHHHHHHHHHHHH	20.12	21712546
277	Ubiquitination	DILMGVLKEVVRQRS HHHHHHHHHHHHHCC	46.16	33845483
284	Phosphorylation	KEVVRQRSDLKVIVM HHHHHHCCCCEEEEE	38.67	25907765
292	Phosphorylation	DLKVIVMSATLDAGK CCEEEEEECEECCCC	13.75	20068231
294	Phosphorylation	KVIVMSATLDAGKFQ EEEEEECEECCCCEE	20.19	21406692
323	Nitration	THPVEIFYTPEPERD CCCEEEEECCCCCHH	27.35	-
323	Phosphorylation	THPVEIFYTPEPERD CCCEEEEECCCCCHH	27.35	23312004
324	Phosphorylation	HPVEIFYTPEPERDY CCEEEEECCCCCHHH	15.49	28985074
331	Phosphorylation	TPEPERDYLEAAIRT CCCCCHHHHHHHHHH	16.80	20068231
370	Sumoylation	DEACKRIKREVDDLG HHHHHHHHHHHHHCC	46.68	-
370	Ubiquitination	DEACKRIKREVDDLG HHHHHHHHHHHHHCC	46.68	29967540
384	Acetylation	GPEVGDIKIIPLYST CCCCCCEEEEECCCC	39.05	26051181
384	Sumoylation	GPEVGDIKIIPLYST CCCCCCEEEEECCCC	39.05	-
384	Ubiquitination	GPEVGDIKIIPLYST CCCCCCEEEEECCCC	39.05	21906983
389	Phosphorylation	DIKIIPLYSTLPPQQ CEEEEECCCCCCHHH	8.34	28152594
390	Phosphorylation	IKIIPLYSTLPPQQQ EEEEECCCCCCHHHH	31.02	28152594
391	Phosphorylation	KIIPLYSTLPPQQQQ EEEECCCCCCHHHHH	29.72	28152594
407	Ubiquitination	IFEPPPPKKQNGAIG CCCCCCCCCCCCCCC	73.16	21906983
408	Ubiquitination	FEPPPPKKQNGAIGR CCCCCCCCCCCCCCC	55.56	22817900
445	Acetylation	DPGFAKQKVYNPRIR CCCCCCCCCCCCCCC	46.08	23749302
445	Ubiquitination	DPGFAKQKVYNPRIR CCCCCCCCCCCCCCC	46.08	27667366
455	Phosphorylation	NPRIRVESLLVTAIS CCCCCHHHHHHHHHH	24.93	28122231
462	O-linked_Glycosylation	SLLVTAISKASAQQR HHHHHHHHHHHHHHH	21.50	23301498
462	Phosphorylation	SLLVTAISKASAQQR HHHHHHHHHHHHHHH	21.50	20363803
463	Ubiquitination	LLVTAISKASAQQRA HHHHHHHHHHHHHHC	40.00	21963094
465	O-linked_Glycosylation	VTAISKASAQQRAGR HHHHHHHHHHHHCCC	30.28	23301498
476	Phosphorylation	RAGRAGRTRPGKCFR HCCCCCCCCCCCEEE	40.05	17924679
480	Ubiquitination	AGRTRPGKCFRLYTE CCCCCCCCEEEEEEC	32.65	29967540
488	Acetylation	CFRLYTEKAYKTEMQ EEEEEECCHHHHHCC	49.57	19608861
488	Ubiquitination	CFRLYTEKAYKTEMQ EEEEEECCHHHHHCC	49.57	23000965
490	Phosphorylation	RLYTEKAYKTEMQDN EEEECCHHHHHCCCC	29.52	-
491	Sumoylation	LYTEKAYKTEMQDNT EEECCHHHHHCCCCC	42.75	-
491	Acetylation	LYTEKAYKTEMQDNT EEECCHHHHHCCCCC	42.75	25953088
491	Sumoylation	LYTEKAYKTEMQDNT EEECCHHHHHCCCCC	42.75	-
491	Ubiquitination	LYTEKAYKTEMQDNT EEECCHHHHHCCCCC	42.75	23000965
494	Sulfoxidation	EKAYKTEMQDNTYPE CCHHHHHCCCCCCHH	7.99	28183972
499	Phosphorylation	TEMQDNTYPEILRSN HHCCCCCCHHHHHCC	12.72	-
505	Phosphorylation	TYPEILRSNLGSVVL CCHHHHHCCHHHHHH	32.72	21712546
509	Phosphorylation	ILRSNLGSVVLQLKK HHHCCHHHHHHHHHH	16.54	21712546
515	Ubiquitination	GSVVLQLKKLGIDDL HHHHHHHHHHCCCCE	32.75	21906983
516	Ubiquitination	SVVLQLKKLGIDDLV HHHHHHHHHCCCCEE	61.61	22817900
614	Acetylation	KKAADEAKMRFAHID HHHHHHHHHHEEEEC	28.67	25953088
614	Ubiquitination	KKAADEAKMRFAHID HHHHHHHHHHEEEEC	28.67	29967540
631	Phosphorylation	HLTLLNVYHAFKQNH HHHHHHHHHHHHHCC	6.07	28152594
653	Phosphorylation	DNFINYRSLMSADNV HCCCCHHHHHCCHHH	20.33	23911959
655	Sulfoxidation	FINYRSLMSADNVRQ CCCHHHHHCCHHHHH	3.07	21406390
670	Methylation	QLSRIMDRFNLPRRS HHHHHHHHHCCCCCC	12.65	-
681	Phosphorylation	PRRSTDFTSRDYYIN CCCCCCCCCCHHHHH	26.18	20068231
682	Phosphorylation	RRSTDFTSRDYYINI CCCCCCCCCHHHHHH	24.13	17081983
686	Phosphorylation	DFTSRDYYINIRKAL CCCCCHHHHHHHHHH	7.56	-
695	Phosphorylation	NIRKALVTGYFMQVA HHHHHHHHHHHHEEE	27.32	20058876
707	Phosphorylation	QVAHLERTGHYLTVK EEEEHHCCCCEEEEC	20.95	28152594
710	Phosphorylation	HLERTGHYLTVKDNQ EHHCCCCEEEECCCE	12.86	28152594
712	Phosphorylation	ERTGHYLTVKDNQVV HCCCCEEEECCCEEE	20.53	24719451
730	Acetylation	PSTVLDHKPEWVLYN CCCCCCCCCCEEEEE	44.28	26051181
746	Phosphorylation	FVLTTKNYIRTCTDI EEEECCCHHCCCCCC	8.04	28152594
754	Acetylation	IRTCTDIKPEWLVKI HCCCCCCCHHHHHHH	39.43	23954790
754	Ubiquitination	IRTCTDIKPEWLVKI HCCCCCCCHHHHHHH	39.43	21963094
760	Acetylation	IKPEWLVKIAPQYYD CCHHHHHHHCCHHCC	30.86	26051181
760	Ubiquitination	IKPEWLVKIAPQYYD CCHHHHHHHCCHHCC	30.86	21963094
777	Acetylation	NFPQCEAKRQLDRII CCCHHHHHHHHHHHH	20.55	25953088
777	Ubiquitination	NFPQCEAKRQLDRII CCCHHHHHHHHHHHH	20.55	29967540
786	Acetylation	QLDRIIAKLQSKEYS HHHHHHHHHHCCHHH	36.33	23749302
786	Malonylation	QLDRIIAKLQSKEYS HHHHHHHHHHCCHHH	36.33	26320211
786	Sumoylation	QLDRIIAKLQSKEYS HHHHHHHHHHCCHHH	36.33	28112733
786	Ubiquitination	QLDRIIAKLQSKEYS HHHHHHHHHHCCHHH	36.33	27667366
790	Ubiquitination	IIAKLQSKEYSQY-- HHHHHHCCHHHCC--	47.94	21906983
792	Phosphorylation	AKLQSKEYSQY---- HHHHCCHHHCC----	12.57	27642862
793	Phosphorylation	KLQSKEYSQY----- HHHCCHHHCC-----	24.89	24719451
795	Phosphorylation	QSKEYSQY------- HCCHHHCC-------	18.00	27642862

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 DHX15_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHX15_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 DHX15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SF3B6_HUMAN	SF3B6	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
PABP1_HUMAN	PABPC1	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
HNRPF_HUMAN	HNRNPF	physical	22939629
HNRPQ_HUMAN	SYNCRIP	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
SNW1_HUMAN	SNW1	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
HNRPK_HUMAN	HNRNPK	physical	22939629
RBMX_HUMAN	RBMX	physical	22939629
NOP58_HUMAN	NOP58	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
NOP56_HUMAN	NOP56	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
FBRL_HUMAN	FBL	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
ECSIT_HUMAN	ECSIT	physical	22939629
TF3C1_HUMAN	GTF3C1	physical	22939629
NDUF4_HUMAN	NDUFAF4	physical	22939629
PROF2_HUMAN	PFN2	physical	22939629
T126B_HUMAN	TMEM126B	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
SENP3_HUMAN	SENP3	physical	22939629
EIF2D_HUMAN	EIF2D	physical	22939629
MMGT1_HUMAN	MMGT1	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
ZNT9_HUMAN	SLC30A9	physical	22939629
PCDA2_HUMAN	PCDHA2	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
SRS10_HUMAN	SRSF10	physical	22939629
LBR_HUMAN	LBR	physical	22939629
EBP2_HUMAN	EBNA1BP2	physical	22939629
PEX3_HUMAN	PEX3	physical	22939629
NXF1_HUMAN	NXF1	physical	22939629
FUT8_HUMAN	FUT8	physical	22939629
IWS1_HUMAN	IWS1	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
SPF45_HUMAN	RBM17	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
RBM5_HUMAN	RBM5	physical	22365833
SUGP1_HUMAN	SUGP1	physical	22365833
DDX42_HUMAN	DDX42	physical	22365833
TRA2A_HUMAN	TRA2A	physical	22365833
NKAP_HUMAN	NKAP	physical	22365833
RBM5_HUMAN	RBM5	physical	22569250
MCTS1_HUMAN	MCTS1	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
TMOD3_HUMAN	TMOD3	physical	22863883
ZGPAT_HUMAN	ZGPAT	physical	25416956
SPF45_HUMAN	RBM17	physical	25416956
PINX1_HUMAN	PINX1	physical	24823796
ATX2_HUMAN	ATXN2	physical	26344197
DDX17_HUMAN	DDX17	physical	26344197
DDX43_HUMAN	DDX43	physical	26344197
DDX5_HUMAN	DDX5	physical	26344197
DKC1_HUMAN	DKC1	physical	26344197
DNJC9_HUMAN	DNAJC9	physical	26344197
EBP2_HUMAN	EBNA1BP2	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
K1143_HUMAN	KIAA1143	physical	26344197
MSH2_HUMAN	MSH2	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
NOLC1_HUMAN	NOLC1	physical	26344197
NOP58_HUMAN	NOP58	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP4_HUMAN	PABPC4	physical	26344197
PESC_HUMAN	PES1	physical	26344197
PRP19_HUMAN	PRPF19	physical	26344197
PRP4_HUMAN	PRPF4	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
RBM15_HUMAN	RBM15	physical	26344197
RB15B_HUMAN	RBM15B	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RSU1_HUMAN	RSU1	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
SK2L2_HUMAN	SKIV2L2	physical	26344197
U520_HUMAN	SNRNP200	physical	26344197
RU2A_HUMAN	SNRPA1	physical	26344197
SRS11_HUMAN	SRSF11	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
TDRD3_HUMAN	TDRD3	physical	26344197
TR112_HUMAN	TRMT112	physical	26344197
TTC27_HUMAN	TTC27	physical	26344197
UBP3_HUMAN	USP3	physical	26344197
WDR36_HUMAN	WDR36	physical	26344197
ZYX_HUMAN	ZYX	physical	26344197

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 DHX15_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-132 AND LYS-488, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-15, AND MASSSPECTROMETRY.	19369195 [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-476, AND MASSSPECTROMETRY.	17924679 [Abstract]