DHX9_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DHX9_MOUSE
• UniProt AC: O70133
• Protein Name: ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211}
• Gene Name: Dhx9 {ECO:0000312|MGI:MGI:108177}
• Organism: Mus musculus (Mouse).
• Sequence Length: 1380
• Subcellular Localization: Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor Importin alph
• 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. Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA replication at origins of replication and cell cycle progression. Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (By similarity). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. [PubMed: 22767893 Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition]
• Protein Sequence: MGDIKNFLYAWCGKRKMTPAYEIRAVGNKNRQKFMCEVRVEGFNYAGMGNSTNKKDAQSNAARDFVNYLVRINEVKSEEVPAVGIVPPPPILSDTSDSTASAAEGLPAPMGGPLPPHLALKAEENNSGVESSGYGSPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGERVEPYKVFLSPDLELQLQNVVQELDLEIVPPPVDPSMPVILNIGKLAHFEPSQRQNAVGVVPWSPPQSNWNPWTSSNIDEGPLAYASTEQISMDLKNELTYQMEQDHNLQSVLQERELLPVKKFEAEILEAISSNSVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVAVAERVAYERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVLAYPEVRIVLMSATIDTTMFCEYFFNCPIIEVYGRTFPVQEYFLEDCIQMTQFIPPPKDKKKKDKEDDGGEDDDANCNLICGDEYGPETKLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLENNSHFGSHRYQILPLHSQIPREEQRKVFDPVPDGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFDRLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAIIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMSGEEAEIRFCEQKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVFIDDWIRLQISHEAAACITIRAAMEALVVEVSKQPNIISQLDPVNEHMLNTIRQISRPSAAGINLMIGSVRYGDGPRPPKMARYDNGSGYRRGYGGGGYGGGGYGGGYGSGGFGGGFGSGGGFGGGFNSGGGGFGSGGGGFGSGGGGFGGGGGGFSGGGGGGFGGGRGGGGGGFGGSGGFGNGGGGYGVGGGGYGGGGGGGYGGGSGGYGGGGYGGGEGYSISPNSYRGNYGGGGGGYRGGSQGGYRNNFGGDYRGSSGDYRGSGGGYRGSGGFQRRGYGGGYFGQGRGGGGGGGY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MGDIKNFLYAWC ---CCHHHHHHHHHH	46.52	22826441
14	Acetylation	FLYAWCGKRKMTPAY HHHHHHCCCCCCCHH	45.79	22826441
33	Malonylation	VGNKNRQKFMCEVRV CCCCCCCCEEEEEEE	31.65	26320211
54	Malonylation	GMGNSTNKKDAQSNA CCCCCCCHHHHHHHH	52.71	26320211
93	Phosphorylation	VPPPPILSDTSDSTA CCCCCCCCCCCCCCC	39.29	22006019
96	Phosphorylation	PPILSDTSDSTASAA CCCCCCCCCCCCHHH	34.26	21183079
98	Phosphorylation	ILSDTSDSTASAAEG CCCCCCCCCCHHHCC	26.16	22006019
101	Phosphorylation	DTSDSTASAAEGLPA CCCCCCCHHHCCCCC	28.27	21183079
127	Phosphorylation	LKAEENNSGVESSGY EEHHHCCCCCCCCCC	56.66	25619855
128 (in isoform 2)	Phosphorylation	-	29.36	22324799
131	Phosphorylation	ENNSGVESSGYGSPG HCCCCCCCCCCCCCC	27.02	25619855
132 (in isoform 2)	Phosphorylation	-	23.64	27742792
132	Phosphorylation	NNSGVESSGYGSPGP CCCCCCCCCCCCCCC	23.64	25619855
133 (in isoform 2)	Phosphorylation	-	39.85	27742792
134	Phosphorylation	SGVESSGYGSPGPTW CCCCCCCCCCCCCCC	19.17	25619855
135 (in isoform 2)	Phosphorylation	-	30.78	21149613
136	Phosphorylation	VESSGYGSPGPTWDR CCCCCCCCCCCCCCC	20.42	25521595
137 (in isoform 2)	Phosphorylation	-	48.71	25521595
140	Phosphorylation	GYGSPGPTWDRGANL CCCCCCCCCCCCCCH	46.01	25619855
141 (in isoform 2)	Phosphorylation	-	9.09	25521595
148	Acetylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	23806337
148	Methylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	-
148	Ubiquitination	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	-
148	Malonylation	WDRGANLKDYYSRKE CCCCCCHHHHHCHHH	43.42	26320211
150	Phosphorylation	RGANLKDYYSRKEEQ CCCCHHHHHCHHHHH	11.18	25367039
151	Phosphorylation	GANLKDYYSRKEEQE CCCHHHHHCHHHHHH	16.48	25367039
193	Acetylation	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	-
193	Ubiquitination	RLNQYFQKEKIQGEY HHHHHHHHHHHCCCC	51.59	-
200	Phosphorylation	KEKIQGEYKYTQVGP HHHHCCCCCEEEECC	19.00	26239621
201	Malonylation	EKIQGEYKYTQVGPD HHHCCCCCEEEECCC	37.20	26320211
201	Acetylation	EKIQGEYKYTQVGPD HHHCCCCCEEEECCC	37.20	23954790
212	Phosphorylation	VGPDHNRSFIAEMTI ECCCCCCCHHHHHHH	26.73	21454597
218	Phosphorylation	RSFIAEMTIYIKQLG CCHHHHHHHHHHHHH	11.35	20531401
220	Phosphorylation	FIAEMTIYIKQLGRR HHHHHHHHHHHHHHH	7.90	21454597
238	Ubiquitination	REHGSNKKLAAQSCA HHCCCCHHHHHHHHH	47.83	-
238	Malonylation	REHGSNKKLAAQSCA HHCCCCHHHHHHHHH	47.83	26320211
244	S-palmitoylation	KKLAAQSCALSLVRQ HHHHHHHHHHHHHHH	2.69	28526873
266	Ubiquitination	EAYSGLTKKKEGERV HHHCCCCCCCCCCCC	67.88	-
266	Acetylation	EAYSGLTKKKEGERV HHHCCCCCCCCCCCC	67.88	22826441
323	Phosphorylation	KLAHFEPSQRQNAVG HHHCCCHHHCCCCCE	30.69	17525332
358	Phosphorylation	EGPLAYASTEQISMD CCCCCEEECCEEECH	21.57	26239621
363	Phosphorylation	YASTEQISMDLKNEL EEECCEEECHHHHHH	13.11	26239621
440	Glutathionylation	QNDRAAECNIVVTQP HCCCHHCCCEEEECC	3.45	24333276
440	S-palmitoylation	QNDRAAECNIVVTQP HCCCHHCCCEEEECC	3.45	28526873
451	Phosphorylation	VTQPRRISAVAVAER EECCCCCCEEEEHHH	18.19	24759943
492	Phosphorylation	HASIMFCTVGVLLRK CCEEHHHHHHHHHHH	14.72	21183079
508	Phosphorylation	EAGIRGISHVIVDEI HHHHCCCEEEEEEHH	17.96	-
676	Phosphorylation	QKHLENNSHFGSHRY HHHHHCCCCCCCCCE	31.60	27841257
690	Phosphorylation	YQILPLHSQIPREEQ EEEECCCCCCCHHHH	37.17	22817900
699	Ubiquitination	IPREEQRKVFDPVPD CCHHHHHCCCCCCCC	47.12	-
714	Phosphorylation	GVTKVILSTNIAETS CCEEEEEECCCCCCE	14.32	26643407
715	Phosphorylation	VTKVILSTNIAETSI CEEEEEECCCCCCEE	27.48	26643407
720	Phosphorylation	LSTNIAETSITINDV EECCCCCCEEECCCE	19.19	26643407
721	Phosphorylation	STNIAETSITINDVV ECCCCCCEEECCCEE	14.83	26643407
723	Phosphorylation	NIAETSITINDVVYV CCCCCEEECCCEEEE	17.31	26643407
729	Phosphorylation	ITINDVVYVIDSCKQ EECCCEEEEEHHHCC	7.49	26643407
733	Phosphorylation	DVVYVIDSCKQKVKL CEEEEEHHHCCEEEE	16.46	26643407
748	Phosphorylation	FTAHNNMTNYATVWA EEECCCCCCCHHEEE	27.48	25367039
750	Phosphorylation	AHNNMTNYATVWASK ECCCCCCCHHEEECC	8.42	25367039
859	Ubiquitination	PLGRILAKLPIEPRF HHHHHHHCCCCCCCC	51.88	-
933	Phosphorylation	AWDDARMSGEEAEIR HHHHHHHCCCHHHHH	37.18	22817900
1013	Malonylation	CYHKEKRKILTTEGR CCCHHHCEEEECCCC	53.81	26320211
1026	Acetylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	23806337
1026	Ubiquitination	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	-
1026	Malonylation	GRNALIHKSSVNCPF CCCCEEECCCCCCCC	37.12	26320211
1031	S-palmitoylation	IHKSSVNCPFSSQDM EECCCCCCCCCCCCC	3.18	28526873
1034	Phosphorylation	SSVNCPFSSQDMKYP CCCCCCCCCCCCCCC	16.54	29472430
1035	Phosphorylation	SVNCPFSSQDMKYPS CCCCCCCCCCCCCCC	30.49	29472430
1039	Ubiquitination	PFSSQDMKYPSPFFV CCCCCCCCCCCCEEE	63.40	-
1050	Ubiquitination	PFFVFGEKIRTRAIS CEEEECHHHHHHHHC	37.56	-
1053	Phosphorylation	VFGEKIRTRAISAKG EECHHHHHHHHCCCC	28.11	22817900
1059	Ubiquitination	RTRAISAKGMTLVTP HHHHHCCCCCEECCH	42.28	-
1075	Ubiquitination	QLLLFASKKVQSDGQ HHHHHHCCCCCCCCE	54.24	-
1076	Ubiquitination	LLLFASKKVQSDGQI HHHHHCCCCCCCCEE	42.91	-
1076	Acetylation	LLLFASKKVQSDGQI HHHHHCCCCCCCCEE	42.91	19851971
1116	Phosphorylation	EALVVEVSKQPNIIS HHHHHHHHCCCCHHH	16.44	23140645
1140	Phosphorylation	LNTIRQISRPSAAGI HHHHHHHCCCCCCCC	29.78	24759943
1167	Asymmetric dimethylarginine	PRPPKMARYDNGSGY CCCCCCCCCCCCCCC	35.52	-
1167	Methylation	PRPPKMARYDNGSGY CCCCCCCCCCCCCCC	35.52	24129315
1176	Methylation	DNGSGYRRGYGGGGY CCCCCCCCCCCCCCC	33.91	-
1305	Phosphorylation	YGGGEGYSISPNSYR CCCCCCCCCCCCCCC	27.70	-
1307	Phosphorylation	GGEGYSISPNSYRGN CCCCCCCCCCCCCCC	16.46	-
1312	Methylation	SISPNSYRGNYGGGG CCCCCCCCCCCCCCC	27.05	24129315
1312	Asymmetric dimethylarginine	SISPNSYRGNYGGGG CCCCCCCCCCCCCCC	27.05	-
1323	Asymmetric dimethylarginine	GGGGGGYRGGSQGGY CCCCCCCCCCCCCCC	46.39	-
1323	Methylation	GGGGGGYRGGSQGGY CCCCCCCCCCCCCCC	46.39	24129315
1326	Phosphorylation	GGGYRGGSQGGYRNN CCCCCCCCCCCCCCC	28.60	-
1330	Phosphorylation	RGGSQGGYRNNFGGD CCCCCCCCCCCCCCC	19.59	-
1339	Asymmetric dimethylarginine	NNFGGDYRGSSGDYR CCCCCCCCCCCCCCC	43.17	-
1339	Methylation	NNFGGDYRGSSGDYR CCCCCCCCCCCCCCC	43.17	24129315
1346	Methylation	RGSSGDYRGSGGGYR CCCCCCCCCCCCCCC	37.23	24129315
1346	Asymmetric dimethylarginine	RGSSGDYRGSGGGYR CCCCCCCCCCCCCCC	37.23	-
1353	Asymmetric dimethylarginine	RGSGGGYRGSGGFQR CCCCCCCCCCCCCCC	35.76	-
1353	Methylation	RGSGGGYRGSGGFQR CCCCCCCCCCCCCCC	35.76	24129315
1361	Methylation	GSGGFQRRGYGGGYF CCCCCCCCCCCCCCC	31.72	24129315
1361	Asymmetric dimethylarginine	GSGGFQRRGYGGGYF CCCCCCCCCCCCCCC	31.72	-
1372	Methylation	GGYFGQGRGGGGGGG CCCCCCCCCCCCCCC	32.47	24129315
1372	Asymmetric dimethylarginine	GGYFGQGRGGGGGGG CCCCCCCCCCCCCCC	32.47	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DHX9_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DHX9_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DHX9_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DHX9_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-323, AND MASSSPECTROMETRY.
PubMed: 17525332