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Appears in Networks 2

In-Edges 3

p(HGNC:UBA2) increases complex(a(MESH:Ubiquitin), p(HGNC:UBA3)) View Subject | View Object

One of several E2 enzymes (ubiquitin-carrier proteins or Ubiquitin-Conjugating enzymes [UBCs]) transfers the activated ubiquitin moiety from E1, via an additional high-energy thiol ester intermediate, E2-S~ubiquitin, to the substrate that is specifically bound to an E3, a member of the ubiquitinprotein ligase family of proteins PubMed:14556719

p(INTERPRO:"E3 ubiquitin ligase RBR family") increases complex(a(MESH:Ubiquitin), p(HGNC:UBA3)) View Subject | View Object

Both HECT and RBR E3s are unique in comparison to the RING ligases because they catalyze an additional transthioesterification step, where ubiquitin is transferred from the E2 to the E3 before its conjugation to the protein substrate (Figure 1A) PubMed:24457024

p(INTERPRO:"HECT domain") increases complex(a(MESH:Ubiquitin), p(HGNC:UBA3)) View Subject | View Object

Both HECT and RBR E3s are unique in comparison to the RING ligases because they catalyze an additional transthioesterification step, where ubiquitin is transferred from the E2 to the E3 before its conjugation to the protein substrate (Figure 1A) PubMed:24457024

Out-Edges 3

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.