Search Results
Overview
| Uniprot ID | P27797 |
|---|---|
| Protein Name | Calreticulin |
| Gene Name | CALR |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 111 | DCGGGYVKLFPNSLD |
| 143 | ICGPGTKKVHVIFNY |
| 151 | VHVIFNYKGKNVLIN |
| 153 | VIFNYKGKNVLINKD |
| 159 | GKNVLINKDIRCKDD |
| 207 | WDFLPPKKIKDPDAS |
| 209 | FLPPKKIKDPDASKP |
| 224 | EDWDERAKIDDPTDS |
| 238 | SKPEDWDKPEHIPDP |
| 355 | GVTKAAEKQMKDKQD |
| 360 | AEKQMKDKQDEEQRL |
| 374 | LKEEEEDKKRKEEEE |
| 377 | EEEDKKRKEEEEAED |
| 43 | RWIESKHKSDFGKFV |
| 48 | KHKSDFGKFVLSSGK |
| 55 | KFVLSSGKFYGDEEK |
| 62 | KFYGDEEKDKGLQTS |
| 64 | YGDEEKDKGLQTSQD |
Function
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0036503 | ERAD pathway |
| Cellular Component | GO:0001669 | acrosomal vesicle |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0060473 | cortical granule |
| Cellular Component | GO:0044194 | cytolytic granule |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0071682 | endocytic vesicle lumen |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0044322 | endoplasmic reticulum quality control compartment |
| Cellular Component | GO:0033116 | endoplasmic reticulum-Golgi intermediate compartment membrane |
| Cellular Component | GO:0009897 | external side of plasma membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0098553 | lumenal side of endoplasmic reticulum membrane |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0042824 | MHC class I peptide loading complex |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0030670 | phagocytic vesicle membrane |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:0005840 | ribosome |
| Cellular Component | GO:0033018 | sarcoplasmic reticulum lumen |
| Cellular Component | GO:0005790 | smooth endoplasmic reticulum |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0030246 | carbohydrate binding |
| Molecular Function | GO:0001849 | complement component C1q complex binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042562 | hormone binding |
| Molecular Function | GO:0005178 | integrin binding |
| Molecular Function | GO:0005506 | iron ion binding |
| Molecular Function | GO:0140313 | molecular sequestering activity |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0050681 | nuclear androgen receptor binding |
| Molecular Function | GO:0005049 | nuclear export signal receptor activity |
| Molecular Function | GO:0042277 | peptide binding |
| Molecular Function | GO:0044183 | protein folding chaperone |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0055007 | cardiac muscle cell differentiation |
| Biological Process | GO:0071257 | cellular response to electrical stimulus |
| Biological Process | GO:0071285 | cellular response to lithium ion |
| Biological Process | GO:0098586 | cellular response to virus |
| Biological Process | GO:0090398 | cellular senescence |
| Biological Process | GO:0006874 | intracellular calcium ion homeostasis |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0033144 | negative regulation of intracellular steroid hormone receptor signaling pathway |
| Biological Process | GO:0045665 | negative regulation of neuron differentiation |
| Biological Process | GO:0048387 | negative regulation of retinoic acid receptor signaling pathway |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:1901164 | negative regulation of trophoblast cell migration |
| Biological Process | GO:0042921 | nuclear receptor-mediated glucocorticoid signaling pathway |
| Biological Process | GO:0002502 | peptide antigen assembly with MHC class I protein complex |
| Biological Process | GO:0045787 | positive regulation of cell cycle |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:2000510 | positive regulation of dendritic cell chemotaxis |
| Biological Process | GO:0010595 | positive regulation of endothelial cell migration |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0050766 | positive regulation of phagocytosis |
| Biological Process | GO:1900026 | positive regulation of substrate adhesion-dependent cell spreading |
| Biological Process | GO:0006611 | protein export from nucleus |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0034975 | protein folding in endoplasmic reticulum |
| Biological Process | GO:0034504 | protein localization to nucleus |
| Biological Process | GO:0051604 | protein maturation |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:1904614 | response to biphenyl |
| Biological Process | GO:0032355 | response to estradiol |
| Biological Process | GO:1903416 | response to glycoside |
| Biological Process | GO:1901652 | response to peptide |
| Biological Process | GO:0033574 | response to testosterone |
| Biological Process | GO:0009410 | response to xenobiotic stimulus |
| Biological Process | GO:0007283 | spermatogenesis |
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] 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] 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.
[9] 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.
[10] 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.