Q9UBZ9: DNA repair protein REV1 (REV1)

DNA repair protein REV1 (REV1) is a 1251-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBZ9.

Gene
REV1
Organism
Homo sapiens
Length
1251 residues
Mean pLDDT
66.6
Model
AF-Q9UBZ9-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.6 (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 accurate39%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Bifunctional protein involved in the maintenance of genome stability through translesion DNA synthesis (TLS) and antibody diversification via somatic hypermutation (PubMed:16263170, PubMed:23143872). Functions as a molecular adapter protein at stalled DNA replication, coordinating polymerases recruitment, selection, and switching, in a manner independent of its deoxycytidyl transferase activity (PubMed:23143872). At the site of DNA lesion, recruits and mediates the switch between low-fidelity inserter DNA polymerases, such as POLK, that incorporate nucleotides opposite lesions and the extender DNA polymerase zeta complex which continues DNA synthesis from distorted primer termini…

Subunit structure

Monomer (By similarity). Homodimer (PubMed:23143872). Homotetramer (PubMed:19464298). Interacts (via C-terminal domain) with the DNA polymerase zeta complex which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct, and REV3L forms and stabilizes the DNA polymerase zeta complex before being recruited by REV1 to the DNA lesion site (PubMed:11485998, PubMed:12529368,…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4EXTX-ray1.9 ÅA=1156-1251
6WS0X-ray2.24 ÅHHH=1158-1251
6ASRX-ray2.36 ÅB=998-1040
6WS5X-ray2.47 ÅHHH=1158-1251
3GQCX-ray2.5 ÅA/B/C/D=330-833
4GK0X-ray2.7 ÅE/F=1117-1251
9VGWX-ray2.7 ÅX/Y/Z=1108-1120
4BA9X-ray2.73 ÅA/B/C/D/E/F=1158-1242
3VU7X-ray2.8 ÅH=1140-1251
4GK5X-ray3.21 ÅE/F=1117-1251
2EBWNMRA=44-133
2LSINMRA=1156-1251
2LSKNMRA=1158-1251
2LSYNMRA=1158-1251
2N1GNMRA=1158-1251
5VZMNMRB=933-1040
6AXDNMRA=998-1040

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