Search Results
Overview
| Uniprot ID | P09525 |
|---|---|
| Protein Name | Annexin A4 |
| Gene Name | ANXA4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 100 | QELRRAMKGAGTDEG |
| 184 | DLYEAGEKKWGTDEV |
| 185 | LYEAGEKKWGTDEVK |
| 213 | LHVFDEYKRISQKDI |
| 218 | EYKRISQKDIEQSIK |
| 246 | IVKCMRNKSAYFAEK |
| 253 | KSAYFAEKLYKSMKG |
| 259 | EKLYKSMKGLGTDDN |
| 28 | QTLRKAMKGLGTDED |
| 293 | HFKRLYGKSLYSFIK |
| 300 | KSLYSFIKGDTSGDY |
| 4 | ****MATKGGTVKAA |
| 57 | QEIRTAYKSTIGRDL |
| 9 | ATKGGTVKAASGFNA |
Function
Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0012506 | vesicle membrane |
| Cellular Component | GO:0042589 | zymogen granule membrane |
| 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:0042802 | identical protein binding |
| Molecular Function | GO:0051059 | NF-kappaB binding |
| Molecular Function | GO:0001786 | phosphatidylserine binding |
| Molecular Function | GO:0004859 | phospholipase inhibitor activity |
| Molecular Function | GO:0140416 | transcription regulator inhibitor activity |
| Biological Process | GO:0030855 | epithelial cell differentiation |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0043124 | negative regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0032717 | negative regulation of interleukin-8 production |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0010804 | negative regulation of tumor necrosis factor-mediated signaling pathway |
| Biological Process | GO:0007165 | signal transduction |
Reference
[1] 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.
[2] 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.
[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] 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.
[5] 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.