Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Appears in Networks 4

In-Edges 9

path(MESH:"Alzheimer Disease") negativeCorrelation act(p(HGNC:UBA2)) View Subject | View Object

Finally, there is also evidence for a reduced activity of E1 and E2 enzymes in cerebral cortex samples from AD patients compared to age-matched controls (Lopez Salon et al., 2000). PubMed:14556719

p(HGNC:UBA3) increases act(p(HGNC:UBA2)) View Subject | View Object

Indeed, recent studies have provided insight into the mechanism of E3-mediated activation of E2s by trapping and either co-crystallizing or characterizing by nuclear magnetic resonance (NMR) the unstable and transient complexes between E2~ubiquitin and E3. PubMed:24457024

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

In summary, mechanisms of E2 activation involve the binding of ubiquitin to surfaces on the E2 and/or E3, thereby allowing an optimal conformation of ubiquitin on the E2 surface PubMed:24457024

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

In summary, mechanisms of E2 activation involve the binding of ubiquitin to surfaces on the E2 and/or E3, thereby allowing an optimal conformation of ubiquitin on the E2 surface PubMed:24457024

Out-Edges 6

p(HGNC:UBA2) decreases complex(a(MESH:Ubiquitin), p(HGNC:UBA1)) 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(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(HGNC:UBA2) increases complex(a(MESH:Ubiquitin), p(INTERPRO:"HECT domain")) View Subject | View Object

For the Homologous to the E6-AP C Terminus (HECT) domain E3s, the ubiquitin is transferred once again from the E2 enzyme to an active site Cys residue on the E3 to generate a third high-energy thiol ester intermediate, ubiquitin-S~E3, prior to its transfer to the ligase bound substrate PubMed:14556719

act(p(HGNC:UBA2)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Finally, there is also evidence for a reduced activity of E1 and E2 enzymes in cerebral cortex samples from AD patients compared to age-matched controls (Lopez Salon et al., 2000). PubMed:14556719

p(HGNC:UBA2) increases p(HGNC:HTT, pmod(Ub)) View Subject | View Object

Thus,Huntingtin was found to be ubiquitinated and also to interact with E2-25 kDa (Kalchman et al., 1996). PubMed:14556719

p(HGNC:UBA2) increases bp(GO:"protein ubiquitination") View Subject | View Object

These studies demonstrated that both E2s and E3s can affect the conformation of the ubiquitin on the E2 surface to promote its transfer to the substrate PubMed:24457024

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.