brca1 dependent ub ligase activity
| PAG Title | brca1 dependent ub ligase activity |
| PAG ID | WAG000212 |
| Type | P |
| Source Link |  BioCarta |
| Publication Reference | NA |
| PAG Description | BRCA1 is a breast and ovarian cancer tumor suppressor protein that associates with BARD1 to form a RING/RING heterodimer. The BRCA1/BARD1 RING complex functions as an ubiquitin (Ub) ligase with activity substantially greater than individual BRCA1 or BARD1 subunits. The BRCA1 tumor suppressor forms a heterodimer with the BARD1 protein, and the resulting complex functions as an E3 ubiquitin ligase that catalyzes the synthesis of polyubiquitin chains. UbcH5c and UbcH7 also interact with the BRCA1/BARD1 complex with similar affinity (not shown on this figure). Although the in vivo substrate(s) is not yet known, BRCA1 has been observed to undergo autoubiquitition and is capable of monoubiquititing histones 2A and 2AX in vitro |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 2,952 |
| Information Content | Rich |
| Other IDs | |
| Base PAG ID | WAG000212 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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