Q63HR2: Tensin-2 (TNS2)

Tensin-2 (TNS2) is a 1409-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q63HR2.

Gene
TNS2
Organism
Homo sapiens
Length
1409 residues
Mean pLDDT
58.3
Model
AF-Q63HR2-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 58.3 (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 accurate25%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1…

Subunit structure

Interacts with AXL (PubMed:12470648). Interacts with SYK; leading to its phosphorylation (PubMed:22019427). Interacts with SQSTM1 (via PB1 domain); the interaction leads to sequestration of TNS2 in cytoplasmic aggregates with SQSTM1 and promotes TNS2 ubiquitination and proteasomal degradation (PubMed:25101860)

Subcellular location

Cell junction, focal adhesion, Cell membrane, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3HQCX-ray1.8 ÅA=1264-1409
2DKQNMRA=1263-1409
2KNONMRA=1135-1249
2L6KNMRA=1135-1248
2LOZNMRA=1263-1409

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