Search Results
Overview
| Uniprot ID | P27348 |
|---|---|
| Protein Name | 14-3-3 protein theta |
| Gene Name | YWHAQ |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 103 | TVLELLDKYLIANAT |
| 11 | TELIQKAKLAEQAER |
| 122 | KVFYLKMKGDYFRYL |
| 139 | VACGDDRKQTIDNSQ |
| 158 | EAFDISKKEMQPTHP |
| 49 | NLLSVAYKNVVGGRR |
| 68 | VISSIEQKTDTSDKK |
| 80 | DKKLQLIKDYREKVE |
| 85 | LIKDYREKVESELRS |
| 9 | EKTELIQKAKLAEQA |
Function
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0071889 | 14-3-3 protein binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0044325 | transmembrane transporter binding |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0034766 | negative regulation of monoatomic ion transmembrane transport |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0021762 | substantia nigra development |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.