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BRENDA support

Literature summary for 2.3.2.31 extracted from

  • Dove, K.K.; Olszewski, J.L.; Martino, L.; Duda, D.M.; Wu, X.S.; Miller, D.J.; Reiter, K.H.; Rittinger, K.; Schulman, B.A.; Klevit, R.E.
    Structural studies of HHARI/UbcH7-Ub reveal unique E2-Ub conformational restriction by RBR RING1 (2017), Structure, 25, 890-900 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of ARIH1 in complex with UbcH7-ubiquitin, to 3.2 A resolution. ARIH1 is autoinhibited even in the complex. The ARIH1 UBA-L domain binds to ubiquitin and NEDD8 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y4X5
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General Information

General Information Comment Organism
physiological function a short extension of ARIH1 RING1, Zn2+-loop II, acts as a steric wedge to disrupt closed E2-ubiquitin, resulting in open E2-ubiquitin that favors ubiquitin transfer to the E3 active site Homo sapiens