The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the DesCEND (destruction via C-end degron) pathway. In the DesCEND pathway, C-terminal residues (C-end degrons) in substrates are recognized by Cul2-RING and Cul4-RING E3 ligases, whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation. C-end degrons can be present in full-length proteins, truncated proteins or proteolytically cleaved forms.

The series of molecular signals generated as a consequence of an opioid growth factor receptor binding to its physiological ligand, opioid growth factor (OGF, met-enkephalin). The OGF-OGFr complex leads to the increase in the synthesis of the selective cyclin-dependent kinase (CDK) inhibitor proteins, p12 (POLD4) and p16 (CDKN2A).

Combining with the opioid growth factor (OGF, met-enkephalin) and transmitting the signal across the nuclear membrane. Met-enkephalin is an endogenous opioid peptide that binds to opioid and opioid growth factor receptors, regulating tissue growth in a variety of cellular processes.

The protein catabolic pathway which selectively extracts ER-resident membrane proteins exported to the Golgi and endosomes for degradation by cytosolic proteasomes. It begins with phosphorylation of the ER-resident membrane protein, which triggers export of the protein from the ER to the Golgi and endosomes, followed by polyubiquitination by the Dsc E3 ubiquitin ligase complex and extraction of the ubiquitinated target, and ends with proteasomal degradation.

Binds to and increases a DNA strand exchange activity.

Catalysis of the reaction: 2 Fe3+-siderophore + NAD(+) + H(+) -> 2 Fe2+-siderophore + NADH.

An epigenetic regulation of transcription by physical interaction between a cis-acting element (enhancer, silencer) of one allele on one chromosome and the promoter of the corresponding allele on the homologous chromosome. Transvection can lead to either gene activation or repression.

Binding to a specific RNA molecule to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active.

Catalyzes the reaction: 2 iodide + L-tyrosine + 2 NADP+ = 3,5-diiodo-L-tyrosine + H+ + 2 NADPH. Note that this activity has only been demonstrated in the direction of 3-deiodination. 3-bromo-L-tyrosine and 3-chloro-L-tyrosine can also be used as substrates.

A protein complex that catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA.

The chemical reactions and pathways resulting in the formation of dihydroxy naphthalene (DHN)-melanin.

Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Mn2+(in) = ADP + H+ + Mn2+(out) + phosphate.

The chemical reactions or pathway resulting in the formation of phycocyanobilin, which involves the oxidative cleavage of heme by a heme oxygenase (HO) to form biliverdin IX alpha. Biliverdin IX alpha is subsequently converted to phycocyanobilin by a ferredoxin-dependent oxidoreductase (PCYA).

Binds to and increases the activity of a cysteine-type endopeptidase.

Binds to and increases the activity of an endopeptidase, any enzyme that hydrolyzes nonterminal peptide bonds in polypeptides.

A motor activity driven by an electrochemical proton gradient (proton-motive force). PMF-driven motors are used by bacterial flagella.

The chemical reactions and pathways resulting in the formation of the coenzyme mycofactocin, a variably glycosylated small molecule electron pair carrier derived from the C-terminal valine-tyrosine dipeptide of the ribosomally translated precursor peptide MftA.

OBSOLETE. Catalysis of the reaction: ATP + H2O = ADP + H+ Pi. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.

Ring-like structures located at the nucleolar periphery where several nuclear factors are reversibly aggregated and sequestered during acute heat stress.

An intranuclear focus at which aggregated proteins have been sequestered.