DX39B_RAT - dbPTM
DX39B_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DX39B_RAT
UniProt AC Q63413
Protein Name Spliceosome RNA helicase Ddx39b
Gene Name Ddx39b
Organism Rattus norvegicus (Rat).
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 Orthologous
Protein Cluster
2Acetylation------MAENDVDNE
------CCCCCCCCC
25.05-
13PhosphorylationVDNELLDYEDDEVET
CCCCCCCCCCCCCCC
22.6421373199
32AcetylationDGTEAPAKKDVKGSY
CCCCCCCCCCCCCCE
48.7422902405
36AcetylationAPAKKDVKGSYVSIH
CCCCCCCCCCEEEEE
52.8872533283
38PhosphorylationAKKDVKGSYVSIHSS
CCCCCCCCEEEEECC
19.3527097102
39PhosphorylationKKDVKGSYVSIHSSG
CCCCCCCEEEEECCC
13.5925575281
41PhosphorylationDVKGSYVSIHSSGFR
CCCCCEEEEECCCCH
13.3223984901
44PhosphorylationGSYVSIHSSGFRDFL
CCEEEEECCCCHHHH
30.4123984901
45PhosphorylationSYVSIHSSGFRDFLL
CEEEEECCCCHHHHC
27.9923984901
53AcetylationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3072533285
156SuccinylationFGGLSIKKDEEVLKK
ECCCCCCCCHHHHHH
69.5626843850
162AcetylationKKDEEVLKKNCPHIV
CCCHHHHHHCCCEEE
47.3022902405
172PhosphorylationCPHIVVGTPGRILAL
CCEEEECCHHHHHHH
15.8023984901
188AcetylationRNKSLNLKHIKHFIL
CCCCCCHHHHHHHHH
42.0622902405
218PhosphorylationVQEIFRMTPHEKQVM
HHHHHHCCHHHHHHH
19.7625575281
228PhosphorylationEKQVMMFSATLSKEI
HHHHHHEEECCCHHH
11.4925575281
230PhosphorylationQVMMFSATLSKEIRP
HHHHEEECCCHHHHH
30.3025575281
232PhosphorylationMMFSATLSKEIRPVC
HHEEECCCHHHHHHH
24.7225575281
334AcetylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH
53.9872533263
344PhosphorylationQRRILVATNLFGRGM
HHHHHHHHCCCCCCC
25.6023984901

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 DX39B_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DX39B_RAT !!

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 DX39B_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DX39B_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DX39B_RAT

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Related Literatures of Post-Translational Modification

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