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Protein Page:
eIF4A2 (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
eIF4A2 ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. Belongs to the DEAD box helicase family. eIF4A subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.13; Translation; Helicase; EC 3.6.1.-; Translation initiation
Cellular Component: eukaryotic translation initiation factor 4F complex; cytosol
Molecular Function: protein binding; translation initiation factor activity; ATP-dependent helicase activity; helicase activity; ATP binding
Biological Process: ATP catabolic process; poly(A) tail shortening; cellular protein metabolic process; viral reproduction; translation; RNA metabolic process; cytokine and chemokine mediated signaling pathway; translational initiation; gene expression; regulation of translational initiation; mRNA catabolic process, deadenylation-dependent decay; mRNA metabolic process
Reference #:  Q14240 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent RNA helicase eIF4A-2; BM-010; DDX2B; eIF-4A-II; EIF4A; eIF4A-II; EIF4A2; EIF4F; Eukaryotic initiation factor 4A-II; eukaryotic translation initiation factor 4A, isoform 2; eukaryotic translation initiation factor 4A2; IF4A2
Gene Symbols: EIF4A2
Molecular weight: 46,402 Da
Basal Isoelectric point: 5.33  Predict pI for various phosphorylation states
CST Pathways:  Translation: eIF4E and p70S6K  |  Translational Control
Select Structure to View Below

eIF4A2

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

► Hide Isoforms
 
0 1 D21-ca GPEGMDPdGVIESNW
0 83 Y49-p ESLLRGIyAyGFEkP
0 8 Y51-p LLRGIyAyGFEkPSA
0 111 K55-ub IyAyGFEkPSAIQQR
0 2 K69-ac RAIIPCIkGyDVIAQ
0 39 K69-ub RAIIPCIkGyDVIAQ
0 12 Y71-p IIPCIkGyDVIAQAQ
0 1 - gap
0 1 K119 ELAQQIQKVILALGD
0 2 K147-ub NVRNEMQkLQAEAPH
0 1 T159-p APHIVVGtPGRVFDM
0 3 K175-ub NRRYLSPkWIKMFVL
0 1 K194 EMLSRGFKDQIYEIF
0 1 K194-ub EMLSRGFkDQIYEIF
0 1 T219-p LLSATMPtDVLEVTK
0 2 K227-ub DVLEVTKkFMRDPIR
0 1 K239 PIRILVKKEELTLEG
0 28 K285-ub IFLNTRRkVDWLTEk
0 24 K292-ub kVDWLTEkMHARDFT
0 2 K310-ub LHGDMDQkERDVIMR
0 6 K370-ub RGGRFGRkGVAINFV
0 4 K382-ub NFVTEEDkRILRDIE
  eIF4A2 iso2  
D22 GPEGMDPDGVIESNW
Y50 ESLLRGIYAYGFEKP
Y52 LLRGIYAYGFEKPSA
K56 IYAYGFEKPSAIQQR
K70 RAIIPCIKGYDVIAQ
K70 RAIIPCIKGYDVIAQ
Y72 IIPCIKGYDVIAQAQ
- gap
K120 ELAQQIQKVILALGD
K148 NVRNEMQKLQAEAPH
T160 APHIVVGTPGRVFDM
K176 NRRYLSPKWIKMFVL
K195 EMLSRGFKDQIYEIF
K195 EMLSRGFKDQIYEIF
T220 LLSATMPTDVLEVTK
K228 DVLEVTKKFMRDPIR
K240 PIRILVKKEELTLEG
K286 IFLNTRRKVDWLTEK
K293 KVDWLTEKMHARDFT
K311 LHGDMDQKERDVIMR
K371 RGGRFGRKGVAINFV
K383 NFVTEEDKRILRDIE
  eIF4A2 iso3  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S12-p LRSLPLFsRELLFPV
K24 FPVLKIQKVILALGD
K52 NVRNEMQKLQAEAPH
T64 APHIVVGTPGRVFDM
K80 NRRYLSPKWIKMFVL
K99 EMLSRGFKDQIYEIF
K99 EMLSRGFKDQIYEIF
T124 LLSATMPTDVLEVTK
K132 DVLEVTKKFMRDPIR
K144 PIRILVKKEELTLEG
K190 IFLNTRRKVDWLTEK
K197 KVDWLTEKMHARDFT
K215 LHGDMDQKERDVIMR
K275 RGGRFGRKGVAINFV
K287 NFVTEEDKRILRDIE
  mouse

 
D21 GPEGMDPDGVIESNW
Y49-p ESLLRGIyAyGFEkP
Y51-p LLRGIyAyGFEkPSA
K55-ub IyAyGFEkPSAIQQR
K69 RAIIPCIKGyDVIAQ
K69-ub RAIIPCIkGyDVIAQ
Y71-p IIPCIkGyDVIAQAQ
- gap
K119-ub ELAQQIQkVILALGD
K147-ub NVRNEMQkLQAEAPH
T159 APHIVVGTPGRVFDM
K175-ub NRRYLSPkWIKMFVL
K194-ac EMLSRGFkDQIYEIF
K194 EMLSRGFKDQIYEIF
T219 LLSATMPTDVLEVTK
K227-ub DVLEVTKkFMRDPIR
K239-ac PIRILVKkEELTLEG
K285-ub IFLNTRRkVDWLTEk
K292-ub kVDWLTEkMHARDFT
K310-ub LHGDMDQkERDVIMR
K370 RGGRFGRKGVAINFV
K382-ub NFVTEEDkRILRDIE
  rat

 
D21 GPEGMDPDGVIESNW
Y49-p ESLLRGIyAYGFEKP
Y51 LLRGIyAYGFEKPSA
K55 IyAYGFEKPSAIQQR
K69 RAIIPCIKGYDVIAQ
K69 RAIIPCIKGYDVIAQ
Y71 IIPCIKGYDVIAQAQ
- gap
K119 ELAQQIQKVILALGD
K147 NVRNEMQKLQAEAPH
T159 APHIVVGTPGRVFDM
K175 NRRYLSPKWIKMFVL
K194 EMLSRGFKDQIYEIF
K194 EMLSRGFKDQIYEIF
T219 LLSATMPTDVLEVTK
K227 DVLEVTKKFMRDPIR
K239 PIRILVKKEELTLEG
K285 IFLNTRRKVDWLTEK
K292 KVDWLTEKMHARDFT
K310 LHGDMDQKERDVIMR
K370 RGGRFGRKGVAINFV
K382 NFVTEEDKRILRDIE
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