Q9Y4R8: Telomere length regulation protein TEL2 homolog (TELO2)

Telomere length regulation protein TEL2 homolog (TELO2) is a 837-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4R8.

Gene
TELO2
Organism
Homo sapiens
Length
837 residues
Mean pLDDT
83.9
Model
AF-Q9Y4R8-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.9 (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 accurate63%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation

Subunit structure

Component of the TTT complex composed of TELO2, TTI1 and TTI2. Interacts with ATM, ATR, MTOR, PRKDC, RUVBL2, TTI1, TTI2, SMG1 and TRRAP. Component of the mTORC1 and mTORC2 complexes. Interacts (phosphorylated form) with PIH1D1 which mediates interaction of TELO2 with the R2TP complex composed of RUVBL1, RUVBL2, PIH1D1, and RPAP3 (PubMed:20864032, PubMed:24656813)

Subcellular location

Cytoplasm, Membrane, Nucleus, Chromosome, telomere

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4PSIX-ray2.45 ÅD/E=489-498
7OLEEM3.41 ÅK=1-455
7F4UEM4.2 ÅA=1-837

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