O43156: TELO2-interacting protein 1 homolog (TTI1)

TELO2-interacting protein 1 homolog (TTI1) is a 1089-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43156.

Gene
TTI1
Organism
Homo sapiens
Length
1089 residues
Mean pLDDT
81.3
Model
AF-O43156-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.3 (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 accurate44%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution6%
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

Subunit structure

Component of the TTT complex composed of TELO2, TTI1 and TTI2 (PubMed:20801936). Interacts with ATM, ATR, MTOR, PRKDC, RUVBL1, SMG1, TELO2, TRRAP and TTI2 (PubMed:20371770, PubMed:20427287, PubMed:20810650). Component of the mTORC1 and mTORC2 complexes (PubMed:23263282, PubMed:36724785). Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex and…

Subcellular location

Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OLEEM3.41 ÅH=1-1089
7F4UEM4.2 ÅB=1-1089

More AlphaFold highlights

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