Search Results
Overview
| Uniprot ID | P20810 |
|---|---|
| Protein Name | Calpastatin |
| Gene Name | CAST |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 132 | GDKKKEKKSLTPAVP |
| 143 | PAVPVESKPDKPSGK |
| 204 | REVTIPPKYRELLAK |
| 212 | YRELLAKKEGITGPP |
| 250 | SPTAAGKKTEKEEST |
| 253 | AAGKKTEKEESTEVL |
| 261 | EESTEVLKAQSAGTV |
| 283 | EKKRKVEKDTMSDQA |
| 319 | IKEVDEAKAKEEKLE |
| 396 | TEKTEESKAAAPAPV |
| 43 | EKKSQSTKLSVVHEK |
| 50 | KLSVVHEKKSQEGKP |
| 51 | LSVVHEKKSQEGKPK |
| 58 | KSQEGKPKEHTEPKS |
| 64 | PKEHTEPKSLPKQAS |
| 68 | TEPKSLPKQASDTGS |
| 684 | KKAASSSKAPKNGGK |
| 687 | ASSSKAPKNGGKAKD |
| 691 | KAPKNGGKAKDSAKT |
Function
Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0010859 | calcium-dependent cysteine-type endopeptidase inhibitor activity |
| Molecular Function | GO:0004866 | endopeptidase inhibitor activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:2000675 | negative regulation of type B pancreatic cell apoptotic process |
| Biological Process | GO:1990709 | presynaptic active zone organization |
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] 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.
[5] 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.
[6] 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.
[7] 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.
[8] 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.