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  2. Ubiquitin - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin

    E4 enzymes, or ubiquitin-chain elongation factors, are capable of adding pre-formed polyubiquitin chains to substrate proteins. [60] For example, multiple monoubiquitylation of the tumor suppressor p53 by Mdm2 [61] can be followed by addition of a polyubiquitin chain using p300 and CBP. [62] [63]

  3. LUBAC - Wikipedia

    en.wikipedia.org/wiki/LUBAC

    Linear ubiquitin chain assembly complex (LUBAC) is a multi-protein complex and the only known E3 ubiquitin ligase able to conjugate ubiquitin in a head-to-tail manner to generate linear (M1-linked) polyubiquitin chains.

  4. Ubiquitin C - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_C

    7316 22190 Ensembl ENSG00000150991 ENSMUSG00000008348 UniProt P0CG48 P0CG50 RefSeq (mRNA) NM_021009 NM_019639 RefSeq (protein) NP_066289 NP_062613 Location (UCSC) Chr 12: 124.91 – 124.92 Mb Chr 5: 125.46 – 125.47 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along ...

  5. Ubiquitin ligase - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_ligase

    Monoubiquitination also can regulate cytosolic protein localization. For example, the E3 ligase MDM2 ubiquitylates p53 either for degradation (K48 polyubiquitin chain), or for nuclear export (monoubiquitylation). These events occur in a concentration dependent fashion, suggesting that modulating E3 ligase concentration is a cellular regulatory ...

  6. Ubiquitin-conjugating enzyme - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-conjugating_enzyme

    Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target ...

  7. Endoplasmic-reticulum-associated protein degradation

    en.wikipedia.org/wiki/Endoplasmic-reticulum...

    Following successive addition of ubiquitin molecules to lysine residues of the previously attached ubiquitin, a polyubiquitin chain is formed. A polyubiquitinated protein is produced and this is recognized by specific subunits in the 19S capping complexes of the 26S proteasome.

  8. McConnell on screaming matches with Trump: ‘We had a candid ...

    www.aol.com/mcconnell-screaming-matches-trump...

    Former Senate Republican Leader Mitch McConnell (Ky.) said he had “candid” conversations with President Trump when asked about reports that he and Trump got into “screaming matches” during ...

  9. Deubiquitinating enzyme - Wikipedia

    en.wikipedia.org/wiki/Deubiquitinating_enzyme

    The chains may be produced by the E1-E2-E3 machinery in the cell free from any substrate protein. Another source of free polyubiquitin is the product of ubiquitin-substrate cleavage. If DUBs cleave the base of the polyubiquitin chain that is attached to a protein, the whole chain will become free and needs to be recycled by DUBs. [2]