DX39B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DX39B_MOUSE
• UniProt AC: Q9Z1N5
• Protein Name: Spliceosome RNA helicase Ddx39b
• Gene Name: Ddx39b
• Organism: Mus musculus (Mouse).
• Sequence Length: 428
• Subcellular Localization: Nucleus. Nucleus speckle. Cytoplasm. Can translocate to the cytoplasm in the presence of MX1..
• Protein Description: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability (By similarity).; Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly (By similarity)..
• Protein Sequence: MAENDVDNELLDYEDDEVETAAGADGTEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR

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
2	Acetylation	------MAENDVDNE ------CCCCCCCCC	25.05	-
13	Phosphorylation	VDNELLDYEDDEVET CCCCCCCCCCCCCCC	22.64	25619855
20	Phosphorylation	YEDDEVETAAGADGT CCCCCCCCCCCCCCC	27.30	30387612
36	Acetylation	APAKKDVKGSYVSIH CCCCCCCCCCEEEEE	52.88	-
36	Ubiquitination	APAKKDVKGSYVSIH CCCCCCCCCCEEEEE	52.88	22790023
36	Malonylation	APAKKDVKGSYVSIH CCCCCCCCCCEEEEE	52.88	26320211
38	Phosphorylation	AKKDVKGSYVSIHSS CCCCCCCCEEEEECC	19.35	26824392
39	Phosphorylation	KKDVKGSYVSIHSSG CCCCCCCEEEEECCC	13.59	28833060
41	Phosphorylation	DVKGSYVSIHSSGFR CCCCCEEEEECCCCH	13.32	23684622
44	Phosphorylation	GSYVSIHSSGFRDFL CCEEEEECCCCHHHH	30.41	28833060
45	Phosphorylation	SYVSIHSSGFRDFLL CEEEEECCCCHHHHC	27.99	28066266
53	Ubiquitination	GFRDFLLKPELLRAI CCHHHHCCHHHHHHH	38.30	22790023
131	Ubiquitination	ELAFQISKEYERFSK HHHHHHHHHHHHHHH	66.98	22790023
138	Acetylation	KEYERFSKYMPNVKV HHHHHHHHHCCCCEE	42.74	22826441
155	Ubiquitination	FFGGLSIKKDEEVLK EECCCCCCCCHHHHH	51.28	22790023
163	Malonylation	KDEEVLKKNCPHIVV CCHHHHHHCCCEEEE	60.67	26320211
172	Phosphorylation	CPHIVVGTPGRILAL CCEEEECCHHHHHHH	15.80	26824392
183	Ubiquitination	ILALARNKSLNLKHI HHHHHCCCCCCHHHH	51.25	27667366
184	Phosphorylation	LALARNKSLNLKHIK HHHHCCCCCCHHHHH	26.49	27681418
188	Acetylation	RNKSLNLKHIKHFIL CCCCCCHHHHHHHHH	42.06	23806337
188	Malonylation	RNKSLNLKHIKHFIL CCCCCCHHHHHHHHH	42.06	26320211
191	Acetylation	SLNLKHIKHFILDEC CCCHHHHHHHHHHHH	31.98	22826441
222	Acetylation	FRMTPHEKQVMMFSA HHCCHHHHHHHHEEE	45.20	22826441
228	Phosphorylation	EKQVMMFSATLSKEI HHHHHHEEECCCHHH	11.49	29895711
230	Phosphorylation	QVMMFSATLSKEIRP HHHHEEECCCHHHHH	30.30	29895711
232	Phosphorylation	MMFSATLSKEIRPVC HHEEECCCHHHHHHH	24.72	29895711
239	S-nitrosylation	SKEIRPVCRKFMQDP CHHHHHHHHHHCCCC	4.31	24926564
241	Acetylation	EIRPVCRKFMQDPME HHHHHHHHHCCCCCE	39.81	-
241	Ubiquitination	EIRPVCRKFMQDPME HHHHHHHHHCCCCCE	39.81	22790023
255	Phosphorylation	EIFVDDETKLTLHGL EEEECCCCEEEECHH	38.05	20469934
258	Phosphorylation	VDDETKLTLHGLQQY ECCCCEEEECHHHHE	20.47	20469934
265	Phosphorylation	TLHGLQQYYVKLKDN EECHHHHEEEECCCC	9.39	20469934
266	Phosphorylation	LHGLQQYYVKLKDNE ECHHHHEEEECCCCH	6.18	20469934
268	Ubiquitination	GLQQYYVKLKDNEKN HHHHEEEECCCCHHH	33.43	22790023
328	Phosphorylation	MPQEERLSRYQQFKD CCHHHHHHHHHHHHH	34.85	29176673
334	Ubiquitination	LSRYQQFKDFQRRIL HHHHHHHHHHHHHHH	53.98	22790023

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

Oops, there are no upstream regulatory protein records of DX39B_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DX39B_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 DX39B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLK1_MOUSE	Plk1	physical	21637952

Drug and Disease Associations

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