Search Results
Overview
| Uniprot ID | P04083 |
|---|---|
| Protein Name | Annexin A1 |
| Gene Name | ANXA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 128 | DELRAAMKGLGTDED |
| 166 | ELKRDLAKDITSDTS |
| 185 | NALLSLAKGDRSEDF |
| 214 | YEAGERRKGTDVNVF |
| 245 | QKYTKYSKHDMNKVL |
| 250 | YSKHDMNKVLDLELK |
| 257 | KVLDLELKGDIEKCL |
| 262 | ELKGDIEKCLTAIVK |
| 274 | IVKCATSKPAFFAEK |
| 281 | KPAFFAEKLHQAMKG |
| 287 | EKLHQAMKGVGTRHK |
| 29 | VQTVKSSKGGPGSAV |
| 312 | EIDMNDIKAFYQKMY |
| 58 | LHKAIMVKGVDEATI |
| 71 | TIIDILTKRNNAQRQ |
| 81 | NAQRQQIKAAYLQET |
| 90 | AYLQETGKPLDETLK |
| 97 | KPLDETLKKALTGHL |
Function
Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T cells (PubMed:17008549). Promotes the differentiation of T cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). In the context of antitumor immunity, interacts with FPR1 on dendritic cells allowing for tumor-associated antigens uptake and cross-presentation to T cells to mount an antitumor specific T cell response
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005912 | adherens junction |
| Cellular Component | GO:0016324 | apical plasma membrane |
| Cellular Component | GO:0016323 | basolateral plasma membrane |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0001533 | cornified envelope |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031901 | early endosome membrane |
| Cellular Component | GO:0005768 | endosome |
| 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:0016328 | lateral plasma membrane |
| Cellular Component | GO:0031514 | motile cilium |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0001891 | phagocytic cup |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0042383 | sarcolemma |
| Cellular Component | GO:0031982 | vesicle |
| Cellular Component | GO:0012506 | vesicle membrane |
| Molecular Function | GO:0098641 | cadherin binding involved in cell-cell adhesion |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0005544 | calcium-dependent phospholipid binding |
| Molecular Function | GO:0048306 | calcium-dependent protein binding |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0001786 | phosphatidylserine binding |
| Molecular Function | GO:0019834 | phospholipase A2 inhibitor activity |
| Molecular Function | GO:0005543 | phospholipid binding |
| Molecular Function | GO:0005102 | signaling receptor binding |
| Biological Process | GO:0030036 | actin cytoskeleton organization |
| Biological Process | GO:0002250 | adaptive immune response |
| Biological Process | GO:0046632 | alpha-beta T cell differentiation |
| Biological Process | GO:0007166 | cell surface receptor signaling pathway |
| Biological Process | GO:0071385 | cellular response to glucocorticoid stimulus |
| Biological Process | GO:0035924 | cellular response to vascular endothelial growth factor stimulus |
| Biological Process | GO:0007187 | G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger |
| Biological Process | GO:0071621 | granulocyte chemotaxis |
| Biological Process | GO:0006954 | inflammatory response |
| Biological Process | GO:0045087 | innate immune response |
| Biological Process | GO:0030216 | keratinocyte differentiation |
| Biological Process | GO:0002548 | monocyte chemotaxis |
| Biological Process | GO:0014839 | myoblast migration involved in skeletal muscle regeneration |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0045920 | negative regulation of exocytosis |
| Biological Process | GO:0032717 | negative regulation of interleukin-8 production |
| Biological Process | GO:0045629 | negative regulation of T-helper 2 cell differentiation |
| Biological Process | GO:0042119 | neutrophil activation |
| Biological Process | GO:0097350 | neutrophil clearance |
| Biological Process | GO:0001780 | neutrophil homeostasis |
| Biological Process | GO:0018149 | peptide cross-linking |
| Biological Process | GO:0006909 | phagocytosis |
| Biological Process | GO:0090050 | positive regulation of cell migration involved in sprouting angiogenesis |
| Biological Process | GO:0032743 | positive regulation of interleukin-2 production |
| Biological Process | GO:0033031 | positive regulation of neutrophil apoptotic process |
| Biological Process | GO:0042102 | positive regulation of T cell proliferation |
| Biological Process | GO:0045627 | positive regulation of T-helper 1 cell differentiation |
| Biological Process | GO:0031340 | positive regulation of vesicle fusion |
| Biological Process | GO:0090303 | positive regulation of wound healing |
| Biological Process | GO:0008360 | regulation of cell shape |
| Biological Process | GO:0046883 | regulation of hormone secretion |
| Biological Process | GO:0050727 | regulation of inflammatory response |
| Biological Process | GO:0032652 | regulation of interleukin-1 production |
| Biological Process | GO:0002685 | regulation of leukocyte migration |
| Biological Process | GO:0007165 | signal transduction |
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] 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] 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.
[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.