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Literature summary extracted from

  • Lei, L.; Bandola-Simon, J.; Roche, P.A.
    Ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I (2018), J. Biol. Chem., 293, 3904-3912 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.23 additional information Ube2D1 enzyme knockdown by specific shRNA. Treatment of HeLa cells with Ube2D1 shRNA results in a over 90% reduction in Ube2D1 protein and a 3fold increase in March-I expression, as determined by quantitative immunoblot analysis. The increase in March-I protein expression in Ube2D1 knockdown cells is correlated precisely with reduced ubiquitination of March-I Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.23 S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine Homo sapiens
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[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.23 Homo sapiens P51668
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-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.23 B-lymphocyte
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Homo sapiens
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2.3.2.23 HeLa cell
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Homo sapiens
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.23 S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
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Homo sapiens [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.23 UBE2D1
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Homo sapiens
2.3.2.23 ubiquitin-conjugating enzyme E2 D1
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Homo sapiens

General Information

EC Number General Information Comment Organism
2.3.2.23 malfunction knocking down ubiquitin-conjugating enzyme E2 D1 (Ube2D1) impairs March-I ubiquitination, increased March-I expression, and enhanced March-I-dependent down-regulation of MHC-II proteins Homo sapiens
2.3.2.23 metabolism March-I is ubiquitinated and degraded in the endocytic pathway involving enzyme UBE2D2 Homo sapiens
2.3.2.23 physiological function ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I, which contributes to March-I turnover. March-I is a membrane-bound E3 ubiquitin ligase belonging to the membrane-associated RING-CH (March) family. March-I ubiquitinates and downregulates the expression of major histocompatibility complex (MHC) class II and cluster of differentiation 86 (CD86) in antigen-presenting cells. Molecular mechanism regulating March-I ubiquitination, overview. March-I is not ubiquinated on a lysine residue. March-I E3 ligase activity is not required for its ubiquitination and does not regulate March-I protein expression. March-I does not undergo autoubiquitination. Ube2D1 together with another E3 ubiquitin ligase regulates March-I expression. March-I is oligo-ubiquitinated and undergoes proteolytic degradation Homo sapiens