dbPTM

DHX9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHX9_HUMAN
UniProt AC	Q08211
Protein Name	ATP-dependent RNA helicase A {ECO:0000305}
Gene Name	DHX9 {ECO:0000312\|HGNC:HGNC:2750}
Organism	Homo sapiens (Human).
Sequence Length	1270
Subcellular Localization	Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleoplasmic shuttling protein (PubMed:10198287, PubMed:16375861, PubMed:10207077, PubMed:9162007). Its nuclear im
Protein Description	Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. [PubMed: 9111062]
Protein Sequence	MGDVKNFLYAWCGKRKMTPSYEIRAVGNKNRQKFMCEVQVEGYNYTGMGNSTNKKDAQSNAARDFVNYLVRINEIKSEEVPAFGVASPPPLTDTPDTTANAEGDLPTTMGGPLPPHLALKAENNSEVGASGYGVPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVVEAYSGLTKKKEGETVEPYKVNLSQDLEHQLQNIIQELNLEILPPPEDPSVPVALNIGKLAQFEPSQRQNQVGVVPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQLEQDHDLQAILQERELLPVKKFESEILEAISQNSVVIIRGATGCGKTTQVPQFILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPEVRIVLMSATIDTSMFCEYFFNCPIIEVYGRTYPVQEYFLEDCIQMTHFVPPPKDKKKKDKDDDGGEDDDANCNLICGDEYGPETRLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLEMNPHFGSHRYQILPLHSQIPREEQRKVFDPVPVGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFERLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAVIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAICTIAAATCFPEPFINEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMGGEEAEIRFCEHKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVLVDDWIKLQISHEAAACITGLRAAMEALVVEVTKQPAIISQLDPVNERMLNMIRQISRPSAAGINLMIGSTRYGDGPRPPKMARYDNGSGYRRGGSSYSGGGYGGGYSSGGYGSGGYGGSANSFRAGYGAGVGGGYRGVSRGGFRGNSGGDYRGPSGGYRGSGGFQRGGGRGAYGTGYFGQGRGGGGY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Sumoylation	---MGDVKNFLYAWC ---CCHHHHHHHHHC	46.88	-
5	Ubiquitination	---MGDVKNFLYAWC ---CCHHHHHHHHHC	46.88	-
9	Phosphorylation	GDVKNFLYAWCGKRK CHHHHHHHHHCCCCC	8.23	28796482
12	S-nitrosocysteine	KNFLYAWCGKRKMTP HHHHHHHCCCCCCCC	3.33	-
12	S-nitrosylation	KNFLYAWCGKRKMTP HHHHHHHCCCCCCCC	3.33	22178444
14	Acetylation	FLYAWCGKRKMTPSY HHHHHCCCCCCCCCC	45.79	25953088
14	Methylation	FLYAWCGKRKMTPSY HHHHHCCCCCCCCCC	45.79	-
14	Succinylation	FLYAWCGKRKMTPSY HHHHHCCCCCCCCCC	45.79	23954790
16	2-Hydroxyisobutyrylation	YAWCGKRKMTPSYEI HHHCCCCCCCCCCEE	51.08	-
16	Ubiquitination	YAWCGKRKMTPSYEI HHHCCCCCCCCCCEE	51.08	-
17	Sulfoxidation	AWCGKRKMTPSYEIR HHCCCCCCCCCCEEE	8.49	28183972
18	Phosphorylation	WCGKRKMTPSYEIRA HCCCCCCCCCCEEEE	16.48	21406692
20	Phosphorylation	GKRKMTPSYEIRAVG CCCCCCCCCEEEECC	26.65	23403867
21	Phosphorylation	KRKMTPSYEIRAVGN CCCCCCCCEEEECCC	19.31	20090780
24	Methylation	MTPSYEIRAVGNKNR CCCCCEEEECCCCCC	15.98	-
33	Acetylation	VGNKNRQKFMCEVQV CCCCCCCCEEEEEEE	31.65	26051181
54	2-Hydroxyisobutyrylation	GMGNSTNKKDAQSNA CCCCCCCHHHHHHHH	52.71	-
54	Acetylation	GMGNSTNKKDAQSNA CCCCCCCHHHHHHHH	52.71	25953088
59	Phosphorylation	TNKKDAQSNAARDFV CCHHHHHHHHHHHHH	30.11	24719451
68	Phosphorylation	AARDFVNYLVRINEI HHHHHHHHHHHHHCC	10.98	25884760
76	Sumoylation	LVRINEIKSEEVPAF HHHHHCCCCCCCCCC	45.71	-
76	Ubiquitination	LVRINEIKSEEVPAF HHHHHCCCCCCCCCC	45.71	-
77	Phosphorylation	VRINEIKSEEVPAFG HHHHCCCCCCCCCCC	44.65	30278072
87	Phosphorylation	VPAFGVASPPPLTDT CCCCCCCCCCCCCCC	35.22	25159151
92	Phosphorylation	VASPPPLTDTPDTTA CCCCCCCCCCCCCCC	43.53	30278072
94	Phosphorylation	SPPPLTDTPDTTANA CCCCCCCCCCCCCCC	20.16	30278072
97	Phosphorylation	PLTDTPDTTANAEGD CCCCCCCCCCCCCCC	29.07	30278072
98	Phosphorylation	LTDTPDTTANAEGDL CCCCCCCCCCCCCCC	25.87	30278072
107	Phosphorylation	NAEGDLPTTMGGPLP CCCCCCCCCCCCCCC	36.39	30278072
108	Phosphorylation	AEGDLPTTMGGPLPP CCCCCCCCCCCCCCC	16.33	30278072
120	Methylation	LPPHLALKAENNSEV CCCCEEEEECCCCCC	48.31	23748837
120	Sumoylation	LPPHLALKAENNSEV CCCCEEEEECCCCCC	48.31	-
125	Phosphorylation	ALKAENNSEVGASGY EEEECCCCCCCCCCC	45.28	21945579
130	Phosphorylation	NNSEVGASGYGVPGP CCCCCCCCCCCCCCC	26.98	21945579
132	Phosphorylation	SEVGASGYGVPGPTW CCCCCCCCCCCCCCC	16.68	21945579
138	Phosphorylation	GYGVPGPTWDRGANL CCCCCCCCCCCCCCH	46.01	21945579
146	2-Hydroxyisobutyrylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	-
146	Acetylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	23749302
146	Methylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	24129315
146	Ubiquitination	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	21906983
148	Phosphorylation	RGANLKDYYSRKEEQ CCCCHHHHHCHHHHH	11.18	27273156
149	Phosphorylation	GANLKDYYSRKEEQE CCCHHHHHCHHHHHH	16.48	28152594
150	Phosphorylation	ANLKDYYSRKEEQEV CCHHHHHCHHHHHHH	30.55	28152594
152	Ubiquitination	LKDYYSRKEEQEVQA HHHHHCHHHHHHHHH	60.71	-
160	Phosphorylation	EEQEVQATLESEEVD HHHHHHHHHCCCEEC	17.61	23663014
163	Phosphorylation	EVQATLESEEVDLNA HHHHHHCCCEECCCC	42.01	23663014
177	Phosphorylation	AGLHGNWTLENAKAR CCCCCCCCHHHHHHH	28.35	20068231
182	Acetylation	NWTLENAKARLNQYF CCCHHHHHHHHHHHH	45.69	26051181
188	Phosphorylation	AKARLNQYFQKEKIQ HHHHHHHHHHHHHHC	13.60	28152594
191	Acetylation	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	19608861
191	Methylation	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	19608861
191	Succinylation	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	23954790
191	Ubiquitination	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	19608861
193	2-Hydroxyisobutyrylation	NQYFQKEKIQGEYKY HHHHHHHHHCCCCCE	47.57	-
193	Acetylation	NQYFQKEKIQGEYKY HHHHHHHHHCCCCCE	47.57	25953088
193	Ubiquitination	NQYFQKEKIQGEYKY HHHHHHHHHCCCCCE	47.57	-
199	2-Hydroxyisobutyrylation	EKIQGEYKYTQVGPD HHHCCCCCEEEECCC	37.20	-
199	Acetylation	EKIQGEYKYTQVGPD HHHCCCCCEEEECCC	37.20	19608861
199	Ubiquitination	EKIQGEYKYTQVGPD HHHCCCCCEEEECCC	37.20	19608861
200	Nitration	KIQGEYKYTQVGPDH HHCCCCCEEEECCCC	11.08	-
200	Phosphorylation	KIQGEYKYTQVGPDH HHCCCCCEEEECCCC	11.08	28152594
201	Phosphorylation	IQGEYKYTQVGPDHN HCCCCCEEEECCCCC	16.78	28152594
216	Phosphorylation	RSFIAEMTIYIKQLG CCHHHHHHHHHHHHH	11.35	-
236	2-Hydroxyisobutyrylation	REHGSNKKLAAQSCA HHCCCCHHHHHHHHH	47.83	-
236	Malonylation	REHGSNKKLAAQSCA HHCCCCHHHHHHHHH	47.83	26320211
241	Phosphorylation	NKKLAAQSCALSLVR CHHHHHHHHHHHHHH	9.16	21712546
242	Glutathionylation	KKLAAQSCALSLVRQ HHHHHHHHHHHHHHH	2.69	22555962
245	Phosphorylation	AAQSCALSLVRQLYH HHHHHHHHHHHHHHH	13.29	24719451
251	Phosphorylation	LSLVRQLYHLGVVEA HHHHHHHHHHCHHHH	6.15	28152594
259	Phosphorylation	HLGVVEAYSGLTKKK HHCHHHHHCCCCCCC	6.97	28152594
260	Phosphorylation	LGVVEAYSGLTKKKE HCHHHHHCCCCCCCC	34.08	28152594
263	Phosphorylation	VEAYSGLTKKKEGET HHHHCCCCCCCCCCE	44.32	28152594
264	2-Hydroxyisobutyrylation	EAYSGLTKKKEGETV HHHCCCCCCCCCCEE	67.88	-
264	Acetylation	EAYSGLTKKKEGETV HHHCCCCCCCCCCEE	67.88	25953088
265	Ubiquitination	AYSGLTKKKEGETVE HHCCCCCCCCCCEEC	51.31	-
266	2-Hydroxyisobutyrylation	YSGLTKKKEGETVEP HCCCCCCCCCCEECC	72.94	-
275	Sumoylation	GETVEPYKVNLSQDL CCEECCEECCCCHHH	35.05	-
279	Phosphorylation	EPYKVNLSQDLEHQL CCEECCCCHHHHHHH	19.22	25159151
305	Phosphorylation	LPPPEDPSVPVALNI CCCCCCCCCCEEEEH	51.91	25159151
321	Phosphorylation	KLAQFEPSQRQNQVG HHHCCCCCCCCCCCC	30.69	17525332
333	Phosphorylation	QVGVVPWSPPQSNWN CCCCCCCCCCCCCCC	22.19	26074081
337	Phosphorylation	VPWSPPQSNWNPWTS CCCCCCCCCCCCCCC	49.97	26074081
343	Phosphorylation	QSNWNPWTSSNIDEG CCCCCCCCCCCCCCC	24.43	26074081
344	Phosphorylation	SNWNPWTSSNIDEGP CCCCCCCCCCCCCCC	19.95	26074081
345	Phosphorylation	NWNPWTSSNIDEGPL CCCCCCCCCCCCCCC	30.35	26074081
356	Phosphorylation	EGPLAFATPEQISMD CCCCCCCCHHHCCHH	22.39	26074081
369	Sulfoxidation	MDLKNELMYQLEQDH HHHHHHHHHHHHCCC	1.31	28183972
370	Phosphorylation	DLKNELMYQLEQDHD HHHHHHHHHHHCCCC	23.67	27642862
391	2-Hydroxyisobutyrylation	ERELLPVKKFESEIL HHCCCCCHHHHHHHH	50.21	-
391	Acetylation	ERELLPVKKFESEIL HHCCCCCHHHHHHHH	50.21	30583217
391	Ubiquitination	ERELLPVKKFESEIL HHCCCCCHHHHHHHH	50.21	-
392	Ubiquitination	RELLPVKKFESEILE HCCCCCHHHHHHHHH	55.38	-
417	Acetylation	RGATGCGKTTQVPQF ECCCCCCCCCCCCCH	53.10	26051181
417	Ubiquitination	RGATGCGKTTQVPQF ECCCCCCCCCCCCCH	53.10	-
418	Phosphorylation	GATGCGKTTQVPQFI CCCCCCCCCCCCCHH	14.03	22798277
419	Phosphorylation	ATGCGKTTQVPQFIL CCCCCCCCCCCCHHH	30.93	22798277
434	Methylation	DDFIQNDRAAECNIV HHHHHCCCHHHCCEE	43.15	-
438	Glutathionylation	QNDRAAECNIVVTQP HCCCHHHCCEEEECC	3.45	22555962
438	S-palmitoylation	QNDRAAECNIVVTQP HCCCHHHCCEEEECC	3.45	29575903
443	Phosphorylation	AECNIVVTQPRRISA HHCCEEEECCCCCCE	23.20	20860994
449	Phosphorylation	VTQPRRISAVSVAER EECCCCCCEEEHHHH	22.32	29255136
452	Phosphorylation	PRRISAVSVAERVAF CCCCCEEEHHHHHHH	18.48	29255136
467	Acetylation	ERGEEPGKSCGYSVR HCCCCCCCCCCEEEE	53.97	26051181
467	Ubiquitination	ERGEEPGKSCGYSVR HCCCCCCCCCCEEEE	53.97	-
472	Phosphorylation	PGKSCGYSVRFESIL CCCCCCEEEEHHHCC	7.66	-
490	Phosphorylation	HASIMFCTVGVLLRK CCEEEHHHHHHHHHH	14.72	24667141
497	2-Hydroxyisobutyrylation	TVGVLLRKLEAGIRG HHHHHHHHHHHHHCC	51.12	-
497	Ubiquitination	TVGVLLRKLEAGIRG HHHHHHHHHHHHHCC	51.12	-
506	Phosphorylation	EAGIRGISHVIVDEI HHHHCCCEEEEEEHH	17.96	25106551
596	Acetylation	KDKKKKDKDDDGGED CCCCCCCCCCCCCCC	72.45	26051181
623	Phosphorylation	YGPETRLSMSQLNEK CCHHHCCCHHHCCCC	17.07	20873877
624	Sulfoxidation	GPETRLSMSQLNEKE CHHHCCCHHHCCCCC	3.33	21406390
625	Phosphorylation	PETRLSMSQLNEKET HHHCCCHHHCCCCCC	28.30	20873877
630	Ubiquitination	SMSQLNEKETPFELI CHHHCCCCCCHHHHH	66.85	-
666	Sulfoxidation	GWNLIYTMQKHLEMN CHHHHHHHHHHHHHC	2.54	28183972
672	Sulfoxidation	TMQKHLEMNPHFGSH HHHHHHHHCCCCCCC	13.72	28183972
678	Phosphorylation	EMNPHFGSHRYQILP HHCCCCCCCCEEEEC	12.12	28348404
681	Phosphorylation	PHFGSHRYQILPLHS CCCCCCCEEEECCCC	8.42	30266825
688	Phosphorylation	YQILPLHSQIPREEQ EEEECCCCCCCHHHH	37.17	26657352
697	Ubiquitination	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	21890473
697	Sumoylation	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	-
697	2-Hydroxyisobutyrylation	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	-
697	Acetylation	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	26051181
697	Sumoylation	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	28112733
697	Ubiquitination	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	21890473
697	Ubiquitination	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	21890473
697	Ubiquitination	IPREEQRKVFDPVPV CCHHHHHCCCCCCCC	47.12	21890473
707	Phosphorylation	DPVPVGVTKVILSTN CCCCCCCEEEEEECC	17.42	20860994
737	Acetylation	DSCKQKVKLFTAHNN HHHCCEEEEEEECCC	44.94	25953088
740	Phosphorylation	KQKVKLFTAHNNMTN CCEEEEEEECCCCCC	37.13	28442448
745	Sulfoxidation	LFTAHNNMTNYATVW EEEECCCCCCCHHEE	2.89	28183972
746	Phosphorylation	FTAHNNMTNYATVWA EEECCCCCCCHHEEE	27.48	24719451
748	Phosphorylation	AHNNMTNYATVWASK ECCCCCCCHHEEECC	8.42	27273156
750	Phosphorylation	NNMTNYATVWASKTN CCCCCCHHEEECCCC	13.25	28442448
754	Phosphorylation	NYATVWASKTNLEQR CCHHEEECCCCHHHH	25.05	24719451
755	Acetylation	YATVWASKTNLEQRK CHHEEECCCCHHHHC	33.41	26051181
755	Ubiquitination	YATVWASKTNLEQRK CHHEEECCCCHHHHC	33.41	21890473
773	S-palmitoylation	GRVRPGFCFHLCSRA CCCCCHHHHHHHHHH	2.32	29575903
777	S-palmitoylation	PGFCFHLCSRARFER CHHHHHHHHHHHHHH	1.62	29575903
787	Phosphorylation	ARFERLETHMTPEMF HHHHHHHHHCCHHHH	22.87	20068231
789	Sulfoxidation	FERLETHMTPEMFRT HHHHHHHCCHHHHCC	9.74	21406390
790	Phosphorylation	ERLETHMTPEMFRTP HHHHHHCCHHHHCCC	14.43	28985074
793	Sulfoxidation	ETHMTPEMFRTPLHE HHHCCHHHHCCCHHH	2.65	28183972
796	Phosphorylation	MTPEMFRTPLHEIAL CCHHHHCCCHHHHHH	20.95	-
806	Acetylation	HEIALSIKLLRLGGI HHHHHHHHHHHHCCH	37.79	26051181
806	Ubiquitination	HEIALSIKLLRLGGI HHHHHHHHHHHHCCH	37.79	-
819	Ubiquitination	GIGQFLAKAIEPPPL CHHHHHHHHCCCCCC	52.63	-
849	Phosphorylation	LDANDELTPLGRILA CCCCCCCCHHHHHHH	17.89	-
857	Ubiquitination	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	21890473
857	2-Hydroxyisobutyrylation	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	-
857	Acetylation	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	25953088
857	Ubiquitination	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	21890473
857	Ubiquitination	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	21890473
857	Ubiquitination	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	21890473
943	Acetylation	EIRFCEHKRLNMATL EEEEECCCCCCCHHH	35.97	7674035
947	Sulfoxidation	CEHKRLNMATLRMTW ECCCCCCCHHHHCHH	3.40	21406390
949	Phosphorylation	HKRLNMATLRMTWEA CCCCCCHHHHCHHHH	12.25	29496963
957	Acetylation	LRMTWEAKVQLKEIL HHCHHHHHHHHHHHH	20.99	26051181
957	Ubiquitination	LRMTWEAKVQLKEIL HHCHHHHHHHHHHHH	20.99	21890473
1011	2-Hydroxyisobutyrylation	CYHKEKRKILTTEGR CCCHHHCEEEECCCC	53.81	-
1011	Malonylation	CYHKEKRKILTTEGR CCCHHHCEEEECCCC	53.81	26320211
1011	Ubiquitination	CYHKEKRKILTTEGR CCCHHHCEEEECCCC	53.81	-
1024	2-Hydroxyisobutyrylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	-
1024	Acetylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	19608861
1024	Malonylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	26320211
1024	Methylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	19608861
1024	Ubiquitination	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	19608861
1025	Phosphorylation	RNALIHKSSVNCPFS CCCEEECCCCCCCCC	25.92	23401153
1026	Phosphorylation	NALIHKSSVNCPFSS CCEEECCCCCCCCCC	23.35	30108239
1029	S-nitrosocysteine	IHKSSVNCPFSSQDM EECCCCCCCCCCCCC	3.18	-
1029	S-nitrosylation	IHKSSVNCPFSSQDM EECCCCCCCCCCCCC	3.18	22178444
1032	Phosphorylation	SSVNCPFSSQDMKYP CCCCCCCCCCCCCCC	16.54	30108239
1033	Phosphorylation	SVNCPFSSQDMKYPS CCCCCCCCCCCCCCC	30.49	30108239
1036	Sulfoxidation	CPFSSQDMKYPSPFF CCCCCCCCCCCCCEE	3.30	21406390
1037	Acetylation	PFSSQDMKYPSPFFV CCCCCCCCCCCCEEE	63.40	21466224
1037	Ubiquitination	PFSSQDMKYPSPFFV CCCCCCCCCCCCEEE	63.40	-
1038	Phosphorylation	FSSQDMKYPSPFFVF CCCCCCCCCCCEEEE	11.42	28152594
1040	Phosphorylation	SQDMKYPSPFFVFGE CCCCCCCCCEEEECH	31.11	28152594
1048	Ubiquitination	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	21890473
1048	Acetylation	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	25825284
1048	Ubiquitination	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	21890473
1048	Ubiquitination	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	21890473
1048	Ubiquitination	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	21890473
1057	Ubiquitination	RTRAISAKGMTLVTP HHHHHCCCCCEECCH	42.28	-
1059	Sulfoxidation	RAISAKGMTLVTPLQ HHHCCCCCEECCHHH	2.30	28183972
1063	Phosphorylation	AKGMTLVTPLQLLLF CCCCEECCHHHHHHH	22.76	-
1072	Phosphorylation	LQLLLFASKKVQSDG HHHHHHHCCCCCCCC	26.19	28348404
1073	2-Hydroxyisobutyrylation	QLLLFASKKVQSDGQ HHHHHHCCCCCCCCC	54.24	-
1073	Ubiquitination	QLLLFASKKVQSDGQ HHHHHHCCCCCCCCC	54.24	-
1074	2-Hydroxyisobutyrylation	LLLFASKKVQSDGQI HHHHHCCCCCCCCCE	42.91	-
1074	Acetylation	LLLFASKKVQSDGQI HHHHHCCCCCCCCCE	42.91	26051181
1074	Ubiquitination	LLLFASKKVQSDGQI HHHHHCCCCCCCCCE	42.91	-
1077	Phosphorylation	FASKKVQSDGQIVLV HHCCCCCCCCCEEEE	46.85	-
1101	Phosphorylation	HEAAACITGLRAAME HHHHHHHHHHHHHHH	30.01	24719451
1107	Sulfoxidation	ITGLRAAMEALVVEV HHHHHHHHHHHHHHH	2.78	28183972
1116	Acetylation	ALVVEVTKQPAIISQ HHHHHHHCCCCHHHH	60.50	26051181
1116	Ubiquitination	ALVVEVTKQPAIISQ HHHHHHHCCCCHHHH	60.50	21890473
1139	Phosphorylation	LNMIRQISRPSAAGI HHHHHHHCCCCCCCC	29.78	28450419
1142	Phosphorylation	IRQISRPSAAGINLM HHHHCCCCCCCCCEE	29.64	28450419
1152	O-linked_Glycosylation	GINLMIGSTRYGDGP CCCEEEECCCCCCCC	9.97	23301498
1152	Phosphorylation	GINLMIGSTRYGDGP CCCEEEECCCCCCCC	9.97	20068231
1153	O-linked_Glycosylation	INLMIGSTRYGDGPR CCEEEECCCCCCCCC	23.77	23301498
1153	Phosphorylation	INLMIGSTRYGDGPR CCEEEECCCCCCCCC	23.77	20068231
1155	Phosphorylation	LMIGSTRYGDGPRPP EEEECCCCCCCCCCC	21.47	28152594
1160	Dimethylation	TRYGDGPRPPKMARY CCCCCCCCCCCCCCC	66.73	-
1160	Methylation	TRYGDGPRPPKMARY CCCCCCCCCCCCCCC	66.73	-
1163	Acetylation	GDGPRPPKMARYDNG CCCCCCCCCCCCCCC	48.12	25953088
1163	Ubiquitination	GDGPRPPKMARYDNG CCCCCCCCCCCCCCC	48.12	-
1166	Asymmetric dimethylarginine	PRPPKMARYDNGSGY CCCCCCCCCCCCCCC	35.52	-
1166	Methylation	PRPPKMARYDNGSGY CCCCCCCCCCCCCCC	35.52	-
1167	Phosphorylation	RPPKMARYDNGSGYR CCCCCCCCCCCCCCC	12.29	-
1171	Phosphorylation	MARYDNGSGYRRGGS CCCCCCCCCCCCCCC	38.62	23401153
1173	Phosphorylation	RYDNGSGYRRGGSSY CCCCCCCCCCCCCCC	9.99	22210691
1174	Methylation	YDNGSGYRRGGSSYS CCCCCCCCCCCCCCC	34.00	-
1175	Dimethylation	DNGSGYRRGGSSYSG CCCCCCCCCCCCCCC	45.39	-
1175	Methylation	DNGSGYRRGGSSYSG CCCCCCCCCCCCCCC	45.39	24129315
1178	Phosphorylation	SGYRRGGSSYSGGGY CCCCCCCCCCCCCCC	29.00	30576142
1179	Phosphorylation	GYRRGGSSYSGGGYG CCCCCCCCCCCCCCC	26.96	30576142
1185	Phosphorylation	SSYSGGGYGGGYSSG CCCCCCCCCCCCCCC	18.84	30576142
1194	Phosphorylation	GGYSSGGYGSGGYGG CCCCCCCCCCCCCCC	16.19	22210691
1199	Phosphorylation	GGYGSGGYGGSANSF CCCCCCCCCCCCCCC	23.10	22210691
1207	Dimethylation	GGSANSFRAGYGAGV CCCCCCCCCCCCCCC	27.24	-
1207	Methylation	GGSANSFRAGYGAGV CCCCCCCCCCCCCCC	27.24	-
1210	Phosphorylation	ANSFRAGYGAGVGGG CCCCCCCCCCCCCCC	11.65	27174698
1218	Phosphorylation	GAGVGGGYRGVSRGG CCCCCCCCCCCCCCC	13.89	27174698
1219	Asymmetric dimethylarginine	AGVGGGYRGVSRGGF CCCCCCCCCCCCCCC	42.16	-
1219	Methylation	AGVGGGYRGVSRGGF CCCCCCCCCCCCCCC	42.16	-
1222	Phosphorylation	GGGYRGVSRGGFRGN CCCCCCCCCCCCCCC	28.21	27174698
1223	Dimethylation	GGYRGVSRGGFRGNS CCCCCCCCCCCCCCC	47.01	-
1223	Methylation	GGYRGVSRGGFRGNS CCCCCCCCCCCCCCC	47.01	-
1227	Dimethylation	GVSRGGFRGNSGGDY CCCCCCCCCCCCCCC	46.81	-
1227	Methylation	GVSRGGFRGNSGGDY CCCCCCCCCCCCCCC	46.81	-
1230	Phosphorylation	RGGFRGNSGGDYRGP CCCCCCCCCCCCCCC	47.15	27174698
1234	Phosphorylation	RGNSGGDYRGPSGGY CCCCCCCCCCCCCCC	22.27	27174698
1235	Asymmetric dimethylarginine	GNSGGDYRGPSGGYR CCCCCCCCCCCCCCC	56.11	-
1235	Methylation	GNSGGDYRGPSGGYR CCCCCCCCCCCCCCC	56.11	-
1241	Phosphorylation	YRGPSGGYRGSGGFQ CCCCCCCCCCCCCCC	18.48	22817900
1242	Asymmetric dimethylarginine	RGPSGGYRGSGGFQR CCCCCCCCCCCCCCC	35.76	-
1242	Methylation	RGPSGGYRGSGGFQR CCCCCCCCCCCCCCC	35.76	-
1249	Asymmetric dimethylarginine	RGSGGFQRGGGRGAY CCCCCCCCCCCCCCC	43.38	-
1249	Methylation	RGSGGFQRGGGRGAY CCCCCCCCCCCCCCC	43.38	-
1253	Dimethylation	GFQRGGGRGAYGTGY CCCCCCCCCCCCCCC	29.82	-
1253	Methylation	GFQRGGGRGAYGTGY CCCCCCCCCCCCCCC	29.82	-
1265	Asymmetric dimethylarginine	TGYFGQGRGGGGY-- CCCCCCCCCCCCC--	32.47	-
1265	Methylation	TGYFGQGRGGGGY-- CCCCCCCCCCCCC--	32.47	-

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 DHX9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHX9_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 DHX9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF65_HUMAN	RELA	physical	15355351
ANM1_HUMAN	PRMT1	physical	15084609
TOP2A_HUMAN	TOP2A	physical	12711669
BRCA1_HUMAN	BRCA1	physical	12592385
AKP8L_HUMAN	AKAP8L	physical	11402034
AKP8L_HUMAN	AKAP8L	physical	10748171
NXF1_HUMAN	NXF1	physical	10924507
KHDR1_HUMAN	KHDRBS1	physical	10951562
TBP_HUMAN	TBP	physical	11149922
TF2B_HUMAN	GTF2B	physical	11149922
SMN_HUMAN	SMN1	physical	11149922
GEMI2_HUMAN	GEMIN2	physical	11149922
DDX20_HUMAN	DDX20	physical	11149922
GEMI4_HUMAN	GEMIN4	physical	11149922
XRCC5_HUMAN	XRCC5	physical	15723802
XRCC6_HUMAN	XRCC6	physical	15723802
SND1_HUMAN	SND1	physical	16914450
EWS_HUMAN	EWSR1	physical	16740692
ACTS_HUMAN	ACTA1	physical	11687588
H2AX_HUMAN	H2AFX	physical	15613478
PRKDC_HUMAN	PRKDC	physical	15613478
UBC9_MOUSE	Ube2i	physical	15312759
ILF3_MOUSE	Ilf3	physical	15312759
PIAS2_MOUSE	Pias2	physical	15312759
UBC9_HUMAN	UBE2I	physical	15312759
RPB1_HUMAN	POLR2A	physical	19309309
ACTB_HUMAN	ACTB	physical	19309309
ZMAT3_HUMAN	ZMAT3	physical	18519039
DICER_HUMAN	DICER1	physical	17531811
AGO2_HUMAN	AGO2	physical	17531811
WRN_HUMAN	WRN	physical	15995249
DPOD1_HUMAN	POLD1	physical	15995249
XRCC5_HUMAN	XRCC5	physical	14704337
PRP8_HUMAN	PRPF8	physical	22939629
SSRP1_HUMAN	SSRP1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
NXF1_HUMAN	NXF1	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
ILF3_HUMAN	ILF3	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
RBM8A_HUMAN	RBM8A	physical	22939629
HNRPF_HUMAN	HNRNPF	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
NOP56_HUMAN	NOP56	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
SRRT_HUMAN	SRRT	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
IF6_HUMAN	EIF6	physical	22939629
RALY_HUMAN	RALY	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
LBR_HUMAN	LBR	physical	22939629
H2B1B_HUMAN	HIST1H2BB	physical	22939629
SON_HUMAN	SON	physical	22939629
MVP_HUMAN	MVP	physical	22939629
EMD_HUMAN	EMD	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
NFIA_HUMAN	NFIA	physical	22939629
T126B_HUMAN	TMEM126B	physical	22939629
PSN1_HUMAN	PSEN1	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
NDUF4_HUMAN	NDUFAF4	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
KINH_HUMAN	KIF5B	physical	22939629
TOM70_HUMAN	TOMM70A	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
PPIB_HUMAN	PPIB	physical	22939629
TRI55_HUMAN	TRIM55	physical	22939629
MIRO2_HUMAN	RHOT2	physical	22939629
SUGP2_HUMAN	SUGP2	physical	22939629
RAB5B_HUMAN	RAB5B	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
CAVN1_HUMAN	PTRF	physical	22939629
GLYR1_HUMAN	GLYR1	physical	22939629
HELQ_HUMAN	HELQ	physical	22939629
DDX5_HUMAN	DDX5	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
NUCL_HUMAN	NCL	physical	22751105
ILF3_HUMAN	ILF3	physical	22751105
DSRAD_HUMAN	ADAR	physical	22751105
HNRPU_HUMAN	HNRNPU	physical	22751105
E2AK2_HUMAN	EIF2AK2	physical	19229320
CN166_HUMAN	C14orf166	physical	22863883
RTCB_HUMAN	RTCB	physical	22863883
NELFB_HUMAN	NELFB	physical	22863883
YBOX3_HUMAN	YBX3	physical	22863883
DDX1_HUMAN	DDX1	physical	22863883
ROA1_HUMAN	HNRNPA1	physical	22863883
HNRPM_HUMAN	HNRNPM	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
MAP7_HUMAN	MAP7	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RFC4_HUMAN	RFC4	physical	22863883
RL26L_HUMAN	RPL26L1	physical	22863883
RL27A_HUMAN	RPL27A	physical	22863883
RL27_HUMAN	RPL27	physical	22863883
ABCD3_HUMAN	ABCD3	physical	26344197
THOC4_HUMAN	ALYREF	physical	26344197
EIF1_HUMAN	EIF1	physical	26344197
EIF1B_HUMAN	EIF1B	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
SPTN1_HUMAN	SPTAN1	physical	26344197
TMOD2_HUMAN	TMOD2	physical	26344197
TMOD3_HUMAN	TMOD3	physical	26344197
UBP7_HUMAN	USP7	physical	26344197
MBD2_HUMAN	MBD2	physical	12665568
RPB1_HUMAN	POLR2A	physical	12665568
OCRL_HUMAN	OCRL	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 DHX9_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-191; LYS-199 AND LYS-1024,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-87 AND SER-321, AND MASSSPECTROMETRY.	18669648 [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-321, AND MASSSPECTROMETRY.	17525332 [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-87, AND MASSSPECTROMETRY.	15302935 [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 TYR-1234 AND TYR-1241, ANDMASS SPECTROMETRY.	17081983 [Abstract]