EC Number |
Application |
Reference |
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2.3.2.27 | analysis |
development of a structure decomposition method that utilizes network analysis and computational thermodynamic measures of fold stability changes upon amino acids alterations |
756518 |
2.3.2.27 | medicine |
human coronaviruses antagonize the viral inhibitor p53 via stabilizing RCHY1 and promoting RCHY1-mediated p53 degradation |
758225 |
2.3.2.27 | medicine |
human T lymphotropic virus type 1 trans-activator/oncoprotein, Tax, stimulates ring finger protein RNF8, and E2 conjugating enzymes, Ubc13:Uev1A and Ubc13:Uev2, for TGFbeta-activated kinase TAK1 and i-kappaB kinase IKK activation. In vitro, the combination of Tax and RNF8 greatly stimulates TAK1, IKK, I-kappaBalpha and JNK phosphorylation. In vivo, RNF8 over-expression augments while RNF8 ablation drastically reduces canonical NF-kappaB activation by Tax. Activation of the non-canonical NF-kappaB pathway by Tax, however, is unaffected by the loss of RNF8. Tax greatly stimulates RNF8 and Ubc13:Uev1A/Uev2 to assemble long K63-polyubiquitin chains. Co-transfection of Tax with increasing amounts of RNF8 greatly induces K63-polyubiquitin assembly in a dose-dependent manner |
735148 |
2.3.2.27 | medicine |
hyperactive mutations L51W and K65R are capable of rescuing the ligase activity of two cancer-associated variants, C61G and C64G. BRCA1 that contains both a cancer variation and the hyperactive substitutions activates the E2 Ube2d to build polyubiquitin chains as well as wild-type BRCA1. Both activating substitutions L51W and K65R are necessary to restore activity of the cancer variants to the level seen in wild-type |
758294 |
2.3.2.27 | medicine |
low UBE4B gene expression is associated with poor outcomes in patients with neuroblastoma and with worse outcomes in all patient subgroups. UBE4B protein expression is associated with neuroblastoma tumor differentiation, and decreased UBE4B protein levels are associated with high-risk features. UBE4B protein levels are also associated with levels of phosphorylated ERK |
756870 |
2.3.2.27 | medicine |
mutation D76E has been identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer |
727995 |
2.3.2.27 | medicine |
successive pruning of the RING structure network of cancer-associated E3 enzymes BRCA1, MDM2, and cIAP2 leads to a core for each RING domain. Substitutions of core residues are associated with cancers according to COSMIC catalog. 80% of the residues located in the core RING subnetworks are nonconserved within E3 RING domains. Core residues for BRCA1 are Thr37, Lys38, Ile68 and Leu73 |
756518 |
2.3.2.27 | medicine |
successive pruning of the RING structure network of cancer-associated E3 enzymes BRCA1, MDM2, and cIAP2 leads to a core for each RING domain. Substitutions of core residues are associated with cancers according to COSMIC catalog. 80% of the residues located in the core RING subnetworks are nonconserved within E3 RING domains. Core residues for cIAP2 are Ser566, I567, Val568, Arg600 and Thr601 |
756518 |
2.3.2.27 | medicine |
successive pruning of the RING structure network of cancer-associated E3 enzymes BRCA1, MDM2, and cIAP2 leads to a core for each RING domain. Substitutions of core residues are associated with cancers according to COSMIC catalog. 80% of the residues located in the core RING subnetworks are nonconserved within E3 RING domains. Core residues for MDM2 are Pro437, Asn447, Gly448, Ala460, Cys461, Ile485 |
756518 |
2.3.2.27 | medicine |
the gene encoding RNF43 is upregulated in colon adenocarcinoma as well as in colon adenoma |
692211 |