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Protein Page:
DDX48 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DDX48 ATP-dependent RNA helicase. Component of a splicing- dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Constitutes at least part of the platform anchoring other EJC proteins to spliced mRNAs. Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH/RBM8A heterodimer, thereby trapping the ATP- bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH/RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Belongs to the DEAD box helicase family. eIF4A subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.1.-; EC 3.6.4.13; Helicase; RNA binding protein; RNA splicing; Spliceosome
Chromosomal Location of Human Ortholog: 17q25.3
Cellular Component: membrane; cytoplasm; nucleolus; nuclear speck; nucleus; cytosol
Molecular Function: mRNA binding; protein binding; ATP-dependent RNA helicase activity; poly(A) binding; ATP binding
Biological Process: ATP catabolic process; nuclear mRNA splicing, via spliceosome; poly(A) tail shortening; mRNA transport; positive regulation of translation; RNA metabolic process; cytokine and chemokine mediated signaling pathway; negative regulation of translation; mRNA catabolic process, nonsense-mediated decay; gene expression; embryonic cranial skeleton morphogenesis; rRNA processing; mRNA catabolic process, deadenylation-dependent decay; mRNA metabolic process
Reference #:  P38919 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent RNA helicase DDX48; ATP-dependent RNA helicase eIF4A-3; DDX48; DEAD (Asp-Glu-Ala-Asp) box polypeptide 48; DEAD box protein 48; DKFZp686O16189; eIF-4A-III; eIF4A-III; EIF4A3; eIF4AIII; Eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-like NUK-34; Eukaryotic translation initiation factor 4A isoform 3; eukaryotic translation initiation factor 4A, isoform 3; eukaryotic translation initiation factor 4A3; hNMP 265; IF4A3; KIAA0111; MGC10862; NMP 265; NMP265; Nuclear matrix protein 265; NUK34
Gene Symbols: EIF4A3
Molecular weight: 46,871 Da
Basal Isoelectric point: 6.3  Predict pI for various phosphorylation states
Select Structure to View Below

DDX48

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T3-p _____MAtTATMAts
0 2 T9-p AtTATMAtsGsARKR
0 4 S10-p tTATMAtsGsARKRL
0 12 S12-p ATMAtsGsARKRLLK
0 86 Y54-p EDLLRGIyAyGFEkP
0 9 Y56-p LLRGIyAyGFEkPSA
0 2 K60-ac IyAyGFEkPSAIQQR
0 111 K60-ub IyAyGFEkPSAIQQR
0 1 S84-p DVIAQSQsGTGKTAT
0 4 K152-ub NVGEDIRkLDyGQHV
0 11 Y155-p EDIRkLDyGQHVVAG
1 13 T163-p GQHVVAGtPGRVFDM
0 1 K182-ub SLRTRAIkMLVLDEA
0 1 K195-ub EADEMLNkGFkEQIy
0 2 K198-ub EMLNkGFkEQIyDVy
0 22 Y202-p kGFkEQIyDVyRYLP
0 1 Y205-p kEQIyDVyRYLPPAT
0 1 T247-p LVKRDELtLEGIKQF
0 1 K252 ELtLEGIKQFFVAVE
0 27 K289-ub IFCNTKRkVDWLTEk
0 1 K296-ac kVDWLTEkMREANFT
0 1 K314-ub MHGDMPQkERESIMk
0 1 K321-ac kERESIMkEFRSGAS
0 1 K321-ub kERESIMkEFRSGAS
0 1 K374-ub RSGRYGRkGVAINFV
0 2 K382-ub GVAINFVkNDDIRIL
0 1 K382-sc GVAINFVkNDDIRIL
  mouse

 
A3 _____MAANATMATS
T9 AANATMATSGsARKR
S10 ANATMATSGsARKRL
S12-p ATMATSGsARKRLLK
Y54-p EDLLRGIyAyGFEkP
Y56-p LLRGIyAyGFEkPSA
K60-ac IyAyGFEkPSAIQQR
K60-ub IyAyGFEkPSAIQQR
S84 DVIAQSQSGTGKTAT
K152 NVGEDIRKLDYGQHV
Y155 EDIRKLDYGQHVVAG
T163-p GQHVVAGtPGRVFDM
K182 SLRTRAIKMLVLDEA
K195 EADEMLNKGFKEQIy
K198 EMLNKGFKEQIyDVY
Y202-p KGFKEQIyDVYRYLP
Y205 KEQIyDVYRYLPPAT
T247 LVKRDELTLEGIkQF
K252-ub ELTLEGIkQFFVAVE
K289-ub IFCNTKRkVDWLTEK
K296 kVDWLTEKMREANFT
K314 MHGDMPQKERESIMK
K321 KERESIMKEFRSGAS
K321 KERESIMKEFRSGAS
K374 RSGRYGRKGVAINFV
K382 GVAINFVKNDDIRIL
K382 GVAINFVKNDDIRIL
  rat

 
A3 _____MAATATMATS
T9 AATATMATSGSARKR
S10 ATATMATSGSARKRL
S12 ATMATSGSARKRLLK
Y54-p EDLLRGIyAYGFEkP
Y56 LLRGIyAYGFEkPSA
K60-ac IyAYGFEkPSAIQQR
K60 IyAYGFEKPSAIQQR
S84 DVIAQSQSGTGKTAT
K152 NVGEDIRKLDYGQHV
Y155 EDIRKLDYGQHVVAG
T163 GQHVVAGTPGRVFDM
K182 SLRTRAIKMLVLDEA
K195 EADEMLNKGFKEQIY
K198 EMLNKGFKEQIYDVY
Y202 KGFKEQIYDVYRYLP
Y205 KEQIYDVYRYLPPAT
T247 LVKRDELTLEGIKQF
K252 ELTLEGIKQFFVAVE
K289 IFCNTKRKVDWLTEK
K296 KVDWLTEKMREANFT
K314 MHGDMPQKERESIMk
K321-ac KERESIMkEFRSGAS
K321 KERESIMKEFRSGAS
K374 RSGRYGRKGVAINFV
K382 GVAINFVKNDDIRIL
K382 GVAINFVKNDDIRIL
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