HIF_alpha_*

Protein HIF_alpha_* map

Identifiers
hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
HUGO:HIF1A HGNC:4910 ENTREZ:3091 UNIPROT:Q16665 GENECARDS:HIF1A REACTOME:56516 KEGG:3091 ATLASONC:GC_HIF1A WIKI:HIF1A

Maps_Modules
 EMT  map  / EMT_REGULATORS  map

References
http://www.omicsonline.org/1948-5956/JCST-03-035.php
HIF-1 is the Commander of Gateways to Cancer
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).

HIF_alpha_*@Cytoplasm

References
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).
e_re1253( EMT  map ):
http://www.omicsonline.org/1948-5956/JCST-03-035.php
HIF-1 is the Commander of Gateways to Cancer
e_re408( EMT  map ):
The transcription and synthesis of HIF-1A are constitutive and seem not to be affected by oxygen.
e_re1241( EMT  map ):
PMID:16716598
HIF-1 plays critical roles in angiogenesis during embryonic development and disease pathogenesis


Modifications:
In compartment: Cytoplasm
  1. HIF_alpha_*@Cytoplasm map

Participates in complexes:
In compartment: Nucleus

  1. HIF1B*:​HIF_alpha_*@Nucleus map

Participates in reactions:
As Reactant or Product:

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

  2. Hypoxia@Cytoplasm map map HIF_alpha_*@Cytoplasm map
  3. HIF_alpha_*@Cytoplasm map map HIF1A@Cytoplasm map
  4. HIF_alpha_*@Cytoplasm map map HIF2_alpha_*@Cytoplasm map
  5. HIF_alpha_*@Cytoplasm map map HIF3_alpha_*@Cytoplasm map
  6. NICD co-factors*@Nucleus map map HIF_alpha_*@Cytoplasm map
  7. rHIF1A@Nucleus map map HIF_alpha_*@Cytoplasm map
  8. HIF_alpha_*@Cytoplasm map + HIF1B*@Cytoplasm map map HIF1B*:​HIF_alpha_*@Nucleus map
  9. HIF_alpha_*@Cytoplasm map map degraded

As Catalyser:

  1. gEndothelin1*@Nucleus map map rEndothelin1*@Nucleus map

  2. gID2@Nucleus map map rID2@Nucleus map
  3. gITGB2@Nucleus map map rITGB2@Nucleus map
  4. gVEGFA@Nucleus map map rVEGFA@Nucleus map
  5. gETS1@Nucleus map map rETS1@Nucleus map
  6. gKRT19@Nucleus map map rKRT19@Nucleus map
  7. gKRT18@Nucleus map map rKRT18@Nucleus map
  8. gKRT14@Nucleus map map rKRT14@Nucleus map
  9. gTGFB3@Nucleus map map rTGFB3@Nucleus map
  10. gVEGFR1*@Nucleus map map rVEGFR1*@Nucleus map
  11. gEG-VEGF*@Nucleus map map rEG-VEGF*@Nucleus map
  12. gVimentin*@Nucleus map map rVimentin*@Nucleus map
  13. gTWIST1@Nucleus map map rTWIST1@Nucleus map
  14. gMMP14@Nucleus map map rMMP14@Nucleus map

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