Q92990: Glomulin (GLMN)

Glomulin (GLMN) is a 594-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92990.

Gene
GLMN
Organism
Homo sapiens
Length
594 residues
Mean pLDDT
88.5
Model
AF-Q92990-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.5 (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 accurate73%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Regulatory component of cullin-RING-based SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes (PubMed:22405651, PubMed:22748924). Inhibits E3 ubiquitin ligase activity by binding to RBX1 (via RING domain) and inhibiting its interaction with the E2 ubiquitin-conjugating enzyme CDC34 (PubMed:22405651, PubMed:22748924). Inhibits RBX1-mediated neddylation of CUL1 (PubMed:22405651). Required for normal stability and normal cellular levels of key components of SCF ubiquitin ligase complexes, including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes to the regulation of CCNE1 and MYC levels (By similarity). Essential for normal development of the vasculature…

Subunit structure

Interacts with FKBP4 and FKBP1A (PubMed:11164950, PubMed:12604780, PubMed:8955134). Isoform 1: Interacts with RBX1 (via RING domain) (PubMed:22405651, PubMed:22748924). Identified in complexes that contain RBX1 plus one of the cullins CUL1, CUL2, CUL3, and CUL4A (PubMed:22405651, PubMed:22748924). Identified in a SCF complex composed of CUL1, RBX1, SKP1, FBXW7 and GLMN (PubMed:22405651).…

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4F52X-ray3.0 ÅE/F=1-594

More AlphaFold highlights

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