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Literature summary for 1.14.14.18 extracted from

  • Biswas, C.; Shah, N.; Muthu, M.; La, P.; Fernando, A.P.; Sengupta, S.; Yang, G.; Dennery, P.A.
    Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses (2014), J. Biol. Chem., 289, 26882-26894.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Mus musculus 5634
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 x * 28000, isoform HO-1, SDS-PAGE Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
LNCaP cell
-
 Mus musculus
-
MEF cell
-
 Mus musculus
-

Subunits

Subunits Comment Organism
? x * 28000, isoform HO-1, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
heme oxygenase-1
-
 Mus musculus
HO-1
-
 Mus musculus

Expression

Organism Comment Expression
Mus musculus isoform HO-1 is induced by oxidative stress and cancer up

General Information

General Information Comment Organism
metabolism isoform HO-1 modulates the function of transcriptional factor Nuclear factor erythroid 2-related factor 2 (Nrf2). In oxidative stress, nuclear isoform HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3beta-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus Mus musculus