DX39B_HUMAN - dbPTM
DX39B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DX39B_HUMAN
UniProt AC Q13838
Protein Name Spliceosome RNA helicase DDX39B
Gene Name DDX39B
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization Nucleus. Nucleus speckle. Cytoplasm. Can translocate to the cytoplasm in the presence of MX1. TREX complex assembly seems to occur in regions surrounding nuclear speckles known as perispeckles.
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. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. 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.; 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 with [PubMed:23299939] reporting a stimulatory effect..
Protein Sequence MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR
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		25.0522223895
13PhosphorylationVDNELLDYEDDEVET
CCCCCCCCCCCCCCC		22.6428355574
20PhosphorylationYEDDEVETAAGGDGA
CCCCCCCCCCCCCCC		27.3026552605
32SumoylationDGAEAPAKKDVKGSY
CCCCCCCCCCCCCCE		48.74-
33UbiquitinationGAEAPAKKDVKGSYV
CCCCCCCCCCCCCEE		70.6121890473
33 (in isoform 2)Ubiquitination-70.6121890473
33 (in isoform 1)Ubiquitination-70.6121890473
36AcetylationAPAKKDVKGSYVSIH
CCCCCCCCCCEEEEE		52.8819608861
36UbiquitinationAPAKKDVKGSYVSIH
CCCCCCCCCCEEEEE		52.8821890473
36 (in isoform 2)Ubiquitination-52.8821890473
362-HydroxyisobutyrylationAPAKKDVKGSYVSIH
CCCCCCCCCCEEEEE		52.88-
36SumoylationAPAKKDVKGSYVSIH
CCCCCCCCCCEEEEE		52.8828112733
36 (in isoform 1)Ubiquitination-52.8821890473
38PhosphorylationAKKDVKGSYVSIHSS
CCCCCCCCEEEEECC		19.3523401153
39PhosphorylationKKDVKGSYVSIHSSG
CCCCCCCEEEEECCC		13.5923927012
41PhosphorylationDVKGSYVSIHSSGFR
CCCCCEEEEECCCCH		13.3223401153
44PhosphorylationGSYVSIHSSGFRDFL
CCEEEEECCCCHHHH		30.4123927012
45PhosphorylationSYVSIHSSGFRDFLL
CEEEEECCCCHHHHC		27.9923927012
53AcetylationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH		38.3019608861
53UbiquitinationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH		38.3021906983
53 (in isoform 2)Ubiquitination-38.3021890473
53 (in isoform 1)Ubiquitination-38.3021890473
58MethylationLLKPELLRAIVDCGF
HCCHHHHHHHHHCCC		34.59-
90UbiquitinationMDVLCQAKSGMGKTA
HHHHHHHCCCCCHHH		22.97-
95UbiquitinationQAKSGMGKTAVFVLA
HHCCCCCHHHHHHHH		25.15-
131UbiquitinationELAFQISKEYERFSK
HHHHHHHHHHHHHHH		66.9821906983
1312-HydroxyisobutyrylationELAFQISKEYERFSK
HHHHHHHHHHHHHHH		66.98-
131 (in isoform 1)Ubiquitination-66.9821890473
137PhosphorylationSKEYERFSKYMPNVK
HHHHHHHHHHCCCCE		29.1523898821
138UbiquitinationKEYERFSKYMPNVKV
HHHHHHHHHCCCCEE		42.7421890473
138AcetylationKEYERFSKYMPNVKV
HHHHHHHHHCCCCEE		42.7425953088
138 (in isoform 1)Ubiquitination-42.7421890473
139PhosphorylationEYERFSKYMPNVKVA
HHHHHHHHCCCCEEE		19.3323898821
146 (in isoform 2)Ubiquitination-6.1521890473
153PhosphorylationAVFFGGLSIKKDEEV
EEEECCCCCCCCHHH		35.3221712546
153 (in isoform 2)Ubiquitination-35.3221890473
155SumoylationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH		51.28-
1552-HydroxyisobutyrylationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH		51.28-
156UbiquitinationFGGLSIKKDEEVLKK
ECCCCCCCCHHHHHH		69.56-
162AcetylationKKDEEVLKKNCPHIV
CCCHHHHHHCCCEEE		47.3026051181
162UbiquitinationKKDEEVLKKNCPHIV
CCCHHHHHHCCCEEE		47.3021906983
1622-HydroxyisobutyrylationKKDEEVLKKNCPHIV
CCCHHHHHHCCCEEE		47.30-
162 (in isoform 1)Ubiquitination-47.3021890473
163UbiquitinationKDEEVLKKNCPHIVV
CCHHHHHHCCCEEEE		60.67-
165S-nitrosocysteineEEVLKKNCPHIVVGT
HHHHHHCCCEEEECC		3.40-
165GlutathionylationEEVLKKNCPHIVVGT
HHHHHHCCCEEEECC		3.4022555962
165S-nitrosylationEEVLKKNCPHIVVGT
HHHHHHCCCEEEECC		3.4022178444
165S-palmitoylationEEVLKKNCPHIVVGT
HHHHHHCCCEEEECC		3.4029575903
172PhosphorylationCPHIVVGTPGRILAL
CCEEEECCHHHHHHH		15.8029255136
177 (in isoform 2)Ubiquitination-2.8521890473
183UbiquitinationILALARNKSLNLKHI
HHHHHCCCCCCHHHH		51.25-
1832-HydroxyisobutyrylationILALARNKSLNLKHI
HHHHHCCCCCCHHHH		51.25-
183MalonylationILALARNKSLNLKHI
HHHHHCCCCCCHHHH		51.2526320211
183AcetylationILALARNKSLNLKHI
HHHHHCCCCCCHHHH		51.2526210075
184PhosphorylationLALARNKSLNLKHIK
HHHHCCCCCCHHHHH		26.4930266825
187 (in isoform 2)Phosphorylation-5.3221406692
188AcetylationRNKSLNLKHIKHFIL
CCCCCCHHHHHHHHH		42.0625825284
188UbiquitinationRNKSLNLKHIKHFIL
CCCCCCHHHHHHHHH		42.0619608861
188MalonylationRNKSLNLKHIKHFIL
CCCCCCHHHHHHHHH		42.0626320211
191AcetylationSLNLKHIKHFILDEC
CCCHHHHHHHHHHHH		31.9825825284
191UbiquitinationSLNLKHIKHFILDEC
CCCHHHHHHHHHHHH		31.98-
198GlutathionylationKHFILDECDKMLEQL
HHHHHHHHHHHHHHH		6.4322555962
2002-HydroxyisobutyrylationFILDECDKMLEQLDM
HHHHHHHHHHHHHHH		57.98-
200AcetylationFILDECDKMLEQLDM
HHHHHHHHHHHHHHH		57.9826051181
208MethylationMLEQLDMRRDVQEIF
HHHHHHHHHHHHHHH		31.17-
217SulfoxidationDVQEIFRMTPHEKQV
HHHHHHHCCHHHHHH		4.8130846556
222AcetylationFRMTPHEKQVMMFSA
HHCCHHHHHHHHEEE		45.2026051181
228PhosphorylationEKQVMMFSATLSKEI
HHHHHHEEECCCHHH		11.4920068231
230PhosphorylationQVMMFSATLSKEIRP
HHHHEEECCCHHHHH		30.3020068231
232PhosphorylationMMFSATLSKEIRPVC
HHEEECCCHHHHHHH		24.7220068231
239S-palmitoylationSKEIRPVCRKFMQDP
CHHHHHHHHHHCCCC		4.3129575903
241UbiquitinationEIRPVCRKFMQDPME
HHHHHHHHHCCCCCE		39.8121890473
241AcetylationEIRPVCRKFMQDPME
HHHHHHHHHCCCCCE		39.8125953088
241 (in isoform 1)Ubiquitination-39.8121890473
243SulfoxidationRPVCRKFMQDPMEIF
HHHHHHHCCCCCEEE		5.0521406390
256AcetylationIFVDDETKLTLHGLQ
EEECCCCEEEECHHH		37.11155883
256 (in isoform 2)Ubiquitination-37.1121890473
256SumoylationIFVDDETKLTLHGLQ
EEECCCCEEEECHHH		37.11-
256UbiquitinationIFVDDETKLTLHGLQ
EEECCCCEEEECHHH		37.11-
265PhosphorylationTLHGLQQYYVKLKDN
EECHHHHEEEECCCC		9.3928152594
266PhosphorylationLHGLQQYYVKLKDNE
ECHHHHEEEECCCCH		6.1828152594
268UbiquitinationGLQQYYVKLKDNEKN
HHHHEEEECCCCHHH		33.4321890473
2682-HydroxyisobutyrylationGLQQYYVKLKDNEKN
HHHHEEEECCCCHHH		33.43-
268AcetylationGLQQYYVKLKDNEKN
HHHHEEEECCCCHHH		33.4326051181
268 (in isoform 1)Ubiquitination-33.4321890473
283 (in isoform 2)Ubiquitination-50.7021890473
328PhosphorylationMPQEERLSRYQQFKD
CCHHHHHHHHHHHHH		34.8526074081
330PhosphorylationQEERLSRYQQFKDFQ
HHHHHHHHHHHHHHH		11.8626074081
334AcetylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH		53.9888695
334UbiquitinationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH		53.9821890473
334SumoylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH		53.98-
3342-HydroxyisobutyrylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH		53.98-
334 (in isoform 1)Ubiquitination-53.9821890473
339MethylationQFKDFQRRILVATNL
HHHHHHHHHHHHHCC		18.79-
344PhosphorylationQRRILVATNLFGRGM
HHHHHHHHCCCCCCC		25.6021712546
349MethylationVATNLFGRGMDIERV
HHHCCCCCCCCCEEE		29.90-
349 (in isoform 2)Ubiquitination-29.9021890473
364SulfoxidationNIAFNYDMPEDSDTY
EEEEECCCCCCCCCH		2.4928183972
368PhosphorylationNYDMPEDSDTYLHRV
ECCCCCCCCCHHHHH		30.14-
370PhosphorylationDMPEDSDTYLHRVAR
CCCCCCCCHHHHHHH		31.75-
371PhosphorylationMPEDSDTYLHRVARA
CCCCCCCHHHHHHHC		12.90-
383PhosphorylationARAGRFGTKGLAITF
HHCCCCCCCCEEEEE		21.16-
384UbiquitinationRAGRFGTKGLAITFV
HCCCCCCCCEEEEEE		52.912190698
384 (in isoform 1)Ubiquitination-52.9121890473
392PhosphorylationGLAITFVSDENDAKI
CEEEEEECCCCHHHH		34.7121712546
398AcetylationVSDENDAKILNDVQD
ECCCCHHHHHHHHHH		51.0611793997
398SumoylationVSDENDAKILNDVQD
ECCCCHHHHHHHHHH		51.06-
399 (in isoform 2)Ubiquitination-4.6921890473
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DX39B_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 DX39B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ICP27_HHV8PORF57physical
18974867
THOC2_HUMANTHOC2physical
15998806
THOC5_HUMANTHOC5physical
15998806
THOC1_HUMANTHOC1physical
15998806
THOC3_HUMANTHOC3physical
15998806
THOC6_HUMANTHOC6physical
15998806
THOC4_HUMANALYREFphysical
15998806
THOC7_HUMANTHOC7physical
15998806
STF1_HUMANNR5A1physical
17190602
SMAD4_HUMANSMAD4physical
17190602
NCBP1_HUMANNCBP1physical
17190602
THOC4_HUMANALYREFphysical
17190602
THOC2_HUMANTHOC2physical
17190602
THOC5_HUMANTHOC5physical
17190602
THOC1_HUMANTHOC1physical
17190602
THOC3_HUMANTHOC3physical
17190602
THOC6_HUMANTHOC6physical
17190602
THOC7_HUMANTHOC7physical
17190602
NCBP2_HUMANNCBP2physical
17190602
UIF_HUMANFYTTD1physical
19836239
THOC4_HUMANALYREFphysical
21799930
RAE1L_HUMANRAE1physical
21799930
PYM1_HUMANWIBGphysical
22939629
WDR74_HUMANWDR74physical
22939629
VP33B_HUMANVPS33Bphysical
22939629
UBE3A_HUMANUBE3Aphysical
22939629
IL7RA_HUMANIL7Rphysical
23151878
GSHR_HUMANGSRphysical
22863883
CH60_HUMANHSPD1physical
22863883
RBBP4_HUMANRBBP4physical
22863883
THOC4_HUMANALYREFphysical
23222130
THOC2_HUMANTHOC2physical
23222130
THOC3_HUMANTHOC3physical
23222130
NCBP1_HUMANNCBP1physical
23222130
LUZP4_HUMANLUZP4physical
25662211
OST48_HUMANDDOSTphysical
26344197
ETFA_HUMANETFAphysical
26344197
PHOCN_HUMANMOB4physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
RPN1_HUMANRPN1physical
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 DX39B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-36; LYS-53 AND LYS-188, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-172, AND MASSSPECTROMETRY.

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