RNA HIF1A map

Identifiers
HUGO:HIF1A
hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
HUGO:HIF1A, HGNC:4910, ENTREZ:3091, GENECARDS:GC14P062162
HUGO:HIF1A HGNC:4910 ENTREZ:3091 UNIPROT:Q16665

Maps_Modules
HMC:TUMOR_PROMOTING_INFLAMMATION
HMC:ACTIVATING_INVASION_AND_METASTASIS
 Cancer Associated Fibroblasts  map  / METABOLIC  map
 EMT Senescence  map  / EMT_REGULATORS  map
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death  map  / ANTIOXIDANT_RESPONSE  map
 Regulated Cell Death  map  / APOPTOSIS  map
 Regulated Cell Death  map  / STARVATION_AUTOPHAGY  map
 Regulated Cell Death  map  / DEATH_RECEPTOR_PATHWAYS  map
 Regulated Cell Death  map  / FATTY_ACID_BIOSYNTHESIS  map
 Regulated Cell Death  map  / GLUCOSE_METABOLISM  map
 Regulated Cell Death  map  / RCD_GENES  map
 Innate Immunity  map  / IMMUNOSUPPPRESSIVE_CORE_PATHWAYS  map
 Innate Immunity  map  / MIRNA_TF_IMMUNOSUPPRESSIVE  map

References
PMID:25732824
expression of HIF-1?? was increased in CAFs, with no significant changes for HIF-2?? or HIF-3??
Stabilization of HIF-1?? protein in induced CAF cells downstream of tgfb 5mRNA level is the same)
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).
PMID:26775703
HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death.
PMID_24006507
HIF1a induces MIF expression of macrophages after hypoxia.
IL4+IL13 inhibit MIF expression via inhibition of HIF1a expression.

Modifications:
In compartment: INNATE_IMMUNE_CELL_Cytosol
  1. rHIF1A@INNATE_IMMUNE_CELL_Cytosol map
Participates in complexes:
    Participates in reactions:
    As Reactant or Product:
    1. gHIF1A@INNATE_IMMUNE_CELL_Cytosol map → map rHIF1A@INNATE_IMMUNE_CELL_Cytosol map
    2. rHIF1A@INNATE_IMMUNE_CELL_Cytosol map → map HIF1A@INNATE_IMMUNE_CELL_Cytosol map
    As Catalyser: