Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Spliceosome RNA helicase DDX39B  

UniProtKB / Swiss-Prot ID :  DX39B_HUMAN

Gene Name (Synonyms) : 
DDX39B, BAT1, UAP56  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Nucleus speckle. 

Protein Function :  Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It 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. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and ALYREF/THOC4. 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 and ALYREF/THOC4. 

Protein Sequence MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSE...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAENDV
---
25.05UniProtKB
Link-
13PhosphotyrosineELLDYEDDE
22.64HPRD
Link-
13PhosphotyrosineELLDYEDDE
22.64Phosphositeplus
Link-
33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)APAKKDVKG
70.61Phosphositeplus
Link-
36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKDVKGSYV
52.88Phosphositeplus
Link-
36N6-acetyllysineKKDVKGSYV
52.88HPRD
Link-
36N6-acetyllysineKKDVKGSYV
52.88Phosphositeplus
Link-
36N6-acetyllysine.KKDVKGSYV
52.88UniProtKB
Link-
38PhosphoserineDVKGSYVSI
19.35HPRD
Link-
38PhosphoserineDVKGSYVSI
19.35Phosphositeplus
Link-
39PhosphotyrosineVKGSYVSIH
13.59Phosphositeplus
Link-
41PhosphoserineGSYVSIHSS
13.32HPRD
Link-
41PhosphoserineGSYVSIHSS
13.32PhosphoELM
Link-
41PhosphoserineGSYVSIHSS
13.32Phosphositeplus
Link-
53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DFLLKPELL
38.30Phosphositeplus
Link-
53N6-acetyllysineDFLLKPELL
38.30HPRD
Link-
53N6-acetyllysine.DFLLKPELL
38.30UniProtKB
Link-
131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FQISKEYER
66.98Phosphositeplus
Link-
138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERFSKYMPN
42.74Phosphositeplus
Link-
162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEVLKKNCP
47.30Phosphositeplus
Link-
165S-nitrosocysteineLKKNCPHIV
3.40dbSNO
Link-
165S-nitrosocysteineLKKNCPHIV
3.40HPRD
Link-
172PhosphothreonineIVVGTPGRI
15.80HPRD
Link-
172PhosphothreonineIVVGTPGRI
15.80PhosphoELM
Link-
172PhosphothreonineIVVGTPGRI
15.80Phosphositeplus
Link-
172Phosphothreonine.IVVGTPGRI
15.80UniProtKB
Link-
188N6-acetyllysineSLNLKHIKH
42.06HPRD
Link-
188N6-acetyllysineSLNLKHIKH
42.06Phosphositeplus
Link-
188N6-acetyllysine.SLNLKHIKH
42.06UniProtKB
Link-
228PhosphoserineVMMFSATLS
11.49HPRD
Link-
228PhosphoserineVMMFSATLS
11.49Phosphositeplus
Link-
241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PVCRKFMQD
39.81Phosphositeplus
Link-
268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QYYVKLKDN
33.43Phosphositeplus
Link
334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YQQFKDFQR
53.98Phosphositeplus
Link
384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RFGTKGLAI
52.91Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures