EIF4E

Protein EIF4E map

Identifiers
eukaryotic translation initiation factor 4E
HUGO:EIF4E HGNC:3287 ENTREZ:1977 UNIPROT:P06730 GENECARDS:EIF4E REACTOME:72577 KEGG:1977 ATLASONC:EIF4EID40431ch4q23 WIKI:EIF4E

Maps_Modules
 EMT  map  / EMT_REGULATORS  map
 Apoptosis  map  / AKT_MTOR  map

References
PMID:9878069
Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E.
PMID:9155017
In vitro, Mnk1 rapidly phosphorylates eIF-4E at the physiologically relevant site, Ser209
Phosphorylation of eIF-4E is believed to enhance its affinity for the 5′-cap

EIF4E@Cytoplasm

References
e_re398( EMT  map ):
PMID:9878069
Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E.
PMID:9155017
In vitro, Mnk1 rapidly phosphorylates eIF-4E at the physiologically relevant site, Ser209

EIF4E|​pho@Cytoplasm

References
e_re398( EMT  map ):
PMID:9878069
Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E.
PMID:9155017
In vitro, Mnk1 rapidly phosphorylates eIF-4E at the physiologically relevant site, Ser209
e_re399( EMT  map ):
PMID:13130303
Regulation of HIF-1a protein synthesis
MNK phosphorylates eIF-4E and stimulates its activity directly.
Active eIF-4E increases the rate of HIF1A-mRNA translation into HIF1A protein.
PMID:16887934
PMID:9159130
HIF-1B (ARNT) is constitutively expressed and itsmRNA and protein are maintained at constant levels regardless of oxygen availability
PMID:9278421
HIF-1A protein has a short half-life (t1/2 = 5 min) and is highly regulated by oxygen
PMID:9746763
The transcription and synthesis of HIF-1B are constitutive and seem not to be affected by oxygen.
PMID:7539918
In normoxia, the HIF-1A proteins are rapidly degraded, resulting in essentially no detectable HIF-1A protein.
PMID:8943284
During hypoxia, HIF-1A becomes stabilized and translocates from the cytoplasm to the nucleus, where it dimerizes with HIF-1B and the HIF complex formed becomes transcriptionally active
PMID:1823643
The activated HIF complex then associates with HREs in the regulatory regions of target genes and binds the transcriptional coactivators to induce gene expression.
PMID:15451019
Tight regulation of the stability and subsequent transactivational function of HIF-1A is chiefly controlled by its post-translation modifications, such as hydroxylation, ubiquitination, acetylation, and phosphorylation
The modification of HIF-1A occurs within several domains.
PMID:10403805
PMID:11566883
PMID:12829734
In normoxia, hydroxylation of 2 proline residues and acetylation of a lysine residue in its ODDD promote interaction of HIF-1A with the von Hippel-Lindau (pVHL) ubiquitin E3 ligase complex (Srinivas et al., 1999; Masson et al., 2001).
PMID:12080085
pVHL complex tags HIF-1A with ubiquitin and thereby marks it for degradation by the 26S proteasome.
In addition, hydroxylation of an asparagine residue in the C-TAD inhibits the association of HIF-1A with CBP/p300 and thus inhibits its transcriptional activity (Lando et al., 2002a).


Modifications:
In compartment: Cytoplasm
  1. EIF4E@Cytoplasm map

  2. EIF4E|​pho@Cytoplasm map

Participates in complexes:
In compartment: Cytoplasm

  1. 4E-BP*:​EIF4E@Cytoplasm map

Participates in reactions:
As Reactant or Product:

  1. EIF4E@Cytoplasm map + 4E-BP*@Cytoplasm map map 4E-BP*:​EIF4E@Cytoplasm map

  2. EIF4E@Cytoplasm map + EIF4B|​S422_pho@Cytoplasm map map Capped RNA translation@Cytoplasm map
  3. EIF4E@Cytoplasm map map EIF4E|​pho@Cytoplasm map

As Catalyser:

  1. rHIF1A@Nucleus map map HIF_alpha_*@Cytoplasm map

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