Details of the Target

General Information of Target

Target ID LDTP00049
Target Name Protein TESPA1 (TESPA1)
Gene Name TESPA1
Gene ID 9840
Synonyms
KIAA0748; Protein TESPA1; Thymocyte-expressed positive selection-associated protein 1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINK
IEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLE
TARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSR
IPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSY
VSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRP
PPPHNTPKRNSLDQVVLEVMDKVKEEKQFLQQDSDLGQFSQEDPVPPAEGKKLPTSPYPC
VFCCEEETQQRMSTVLAPSQTLDSNPKVPCCTHSLPIEDPQWSTDPAQIRRELCSLPATN
TETHPAKDETFWKRKSRARKSLFQKNLMGRKVKSLDLSITQQKWKQSVDRPELRRSLSQQ
PQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS
Target Bioclass
Other
Subcellular location
Cytoplasm
Function
Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development. Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment.
Uniprot ID
A2RU30
Ensemble ID
ENST00000316577.12
HGNC ID
HGNC:29109

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
22RV1 SNV: p.Q482R .
A2058 SNV: p.I195L .
KYSE30 Substitution: p.R207E .
LS180 SNV: p.V319A; p.Q338Ter .
NCIH1792 SNV: p.S278Ter .
SKMEL5 SNV: p.S10F; p.W432Ter .
TF1 SNV: p.N59S .

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
ATP probe
 Probe Info  		K322(0.00); K324(0.00)  LDD0199  [1]

References

1 Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases. J Proteome Res. 2022 Aug 5;21(8):2063-2070. doi: 10.1021/acs.jproteome.2c00225. Epub 2022 Jul 12.