Q5U5Q9: BRCA1-A complex subunit RAP80 (Uimc1)

BRCA1-A complex subunit RAP80 (Uimc1) is a 727-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5U5Q9.

Gene
Uimc1
Organism
Mus musculus
Length
727 residues
Mean pLDDT
55.2
Model
AF-Q5U5Q9-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 55.2 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate13%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution18%
Below 50Very low: often disordered regions59%

What pLDDT means and how to read it

Function

Ubiquitin-binding protein. Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19536136). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does…

Subunit structure

Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). In the BRCA1-A complex, interacts directly with ABRAXAS1 (By similarity). Interacts with ESR1 (By similarity).…

Subcellular location

Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3A1QX-ray2.2 ÅC/F=80-120
6GVWX-ray3.75 ÅE/J=275-334

More AlphaFold highlights

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