Q92890: Ubiquitin recognition factor in ER-associated degradation protein 1 (UFD1)

Ubiquitin recognition factor in ER-associated degradation protein 1 (UFD1) is a 307-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92890.

Gene
UFD1
Organism
Homo sapiens
Length
307 residues
Mean pLDDT
74.6
Model
AF-Q92890-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.6 (confident 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 accurate38%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution26%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to RIGI and recruits RNF125…

Subunit structure

Heterodimer with NPLOC4, this heterodimer binds VCP and inhibits Golgi membrane fusion (PubMed:11574150, PubMed:26471729). Interacts with USP13 (PubMed:21571647). Interacts with ZFAND2B; probably through VCP (PubMed:24160817)

Subcellular location

Nucleus, Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5B6CX-ray1.55 ÅB=225-235
7WWQX-ray2.72 ÅB=258-273
9YRCEM2.97 ÅH=1-307
5C1BX-ray3.08 ÅU/V=221-241
9YW2EM3.27 ÅI=1-307
11TAEM3.58 ÅP=1-307
11VEEM3.85 ÅP=1-307
11SYEM4.28 ÅP=1-307
2YUJNMRA=11-193

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