Search Results
Overview
| Uniprot ID | P63104 |
|---|---|
| Protein Name | 14-3-3 protein zeta/delta |
| Gene Name | YWHAZ |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 11 | NELVQKAKLAEQAER |
| 120 | ESKVFYLKMKGDYYR |
| 122 | KVFYLKMKGDYYRYL |
| 138 | EVAAGDDKKGIVDQS |
| 139 | VAAGDDKKGIVDQSQ |
| 157 | QEAFEISKKEMQPTH |
| 158 | EAFEISKKEMQPTHP |
| 3 | *****MDKNELVQKA |
| 49 | NLLSVAYKNVVGARR |
| 68 | VVSSIEQKTEGAEKK |
| 85 | MAREYREKIETELRD |
| 9 | DKNELVQKAKLAEQA |
Function
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:14578935, PubMed:15071501, PubMed:15644438, PubMed:16376338, PubMed:16959763, PubMed:31024343, PubMed:9360956). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35662396). Binding generally results in the modulation of the activity of the binding partner (PubMed:35662396). Promotes cytosolic retention and inactivation of TFEB transcription factor by binding to phosphorylated TFEB (PubMed:35662396). Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (PubMed:16959763). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0072562 | blood microparticle |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0098686 | hippocampal mossy fiber to CA3 synapse |
| Cellular Component | GO:0042470 | melanosome |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0031982 | vesicle |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0050815 | phosphoserine residue binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0019903 | protein phosphatase binding |
| Molecular Function | GO:0140311 | protein sequestering activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0044325 | transmembrane transporter binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0042149 | cellular response to glucose starvation |
| Biological Process | GO:0051683 | establishment of Golgi localization |
| Biological Process | GO:0090168 | Golgi reassembly |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0030324 | lung development |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0045824 | negative regulation of innate immune response |
| Biological Process | GO:1900181 | negative regulation of protein localization to nucleus |
| Biological Process | GO:1904262 | negative regulation of TORC1 signaling |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006468 | protein phosphorylation |
| Biological Process | GO:0070372 | regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:0031647 | regulation of protein stability |
| Biological Process | GO:0090128 | regulation of synapse maturation |
| Biological Process | GO:0003016 | respiratory system process |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0008039 | synaptic target recognition |
| Biological Process | GO:0035148 | tube formation |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] 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.
[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[6] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[7] 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.
[8] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[9] 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.
[10] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[11] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[12] 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.