HIF1B*

Protein HIF1B* map

Identifiers
aryl hydrocarbon receptor nuclear translocator
HUGO:ARNT HGNC:700 ENTREZ:405 UNIPROT:P27540 GENECARDS:ARNT REACTOME:50297 KEGG:405 ATLASONC:ARNTID223ch1q21 WIKI:ARNT

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).
synonym:HIF1beta

HIF1B*@Cytoplasm

References
e_re406( 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_re1242( EMT  map ):
PMID:16716598
HIF-1 plays critical roles in angiogenesis during embryonic development and disease pathogenesis

HIF1B*@Nucleus

References
a_re1200( Apoptosis  map ):
PMID:20308559
bioinformatic prediction
in HCT116, expression of MIR107 precursor decreases ARNT protein abundance
in HCT116, in Hela, in SW480, RNA antisens to MIR107 increases ARNT protein abundance
+ luciferase reporter assay using the 3′UTR of ARNT
in HCT116, knockdown of endogenous miR-107 increased desferrioxamine(hypoxia mimick)-induced VEGF levels, which is rescued by a expression of ARNT lacking its 3′UTR.
in HCT116, pre-miR-107 decreases the ability of HCT116 cells to stimulate endothelial proliferation upon hypoxia (MMT assay)


Modifications:
In compartment: Cytoplasm
  1. HIF1B*@Cytoplasm map

In compartment: Nucleus

  1. HIF1B*@Nucleus map

Participates in complexes:
In compartment: Nucleus

  1. HIF1B*:​HIF_alpha_*@Nucleus map

Participates in reactions:
As Reactant or Product:

  1. rHIF1B*@Nucleus map map HIF1B*@Nucleus map

  2. HIF1A@Nucleus map + HIF1B*@Nucleus map map a_s3082
  3. HIF1B*@Cytoplasm map map Angiogenesis@Nucleus map
  4. rHIF1B*@Nucleus map map HIF1B*@Cytoplasm map
  5. HIF_alpha_*@Cytoplasm map + HIF1B*@Cytoplasm map map HIF1B*:​HIF_alpha_*@Nucleus map

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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