Search Results

Overview

Uniprot IDP26447
Protein NameProtein S100-A4
Gene NameS100A4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
18 VMVSTFHKYSGKEGD
22 TFHKYSGKEGDKFKL
31 GDKFKLNKSELKELL
35 KLNKSELKELLTREL
48 ELPSFLGKRTDEAAF
57 TDEAAFQKLMSNLDS
7 *MACPLEKALDVMVS

Function

Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:16707441, PubMed:23752197, PubMed:30713770). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:16707441). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Also modulates the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (PubMed:23752197). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (PubMed:26654597, PubMed:30713770)

Protein Sequence

10 MACPLEKALD 20 VMVSTFHKYS 30 GKEGDKFKLN 40 KSELKELLTR 50 ELPSFLGKRT 60 DEAAFQKLMS 70 NLDSNRDNEV 80 DFQEYCVFLS 90 CIAMMCNEFF 100 EGFPDKQPRK K

Gene Ontology

Classification GO ID Description
Molecular Function GO:0050786 RAGE receptor binding
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:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Molecular Function GO:0003779 actin binding
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:0042056 chemoattractant activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0046914 transition metal ion binding
Biological Process GO:0001837 epithelial to mesenchymal transition
Biological Process GO:0043123 positive regulation of canonical NF-kappaB 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] 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.

[6] 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.