Search Results

Overview

Uniprot IDP60903
Protein NameProtein S100-A10
Gene NameS100A10
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
23 FHKFAGDKGYLTKED
28 GDKGYLTKEDLRVLM
37 DLRVLMEKEFPGFLE
47 PGFLENQKDPLAVDK
54 KDPLAVDKIMKDLDQ
57 LAVDKIMKDLDQCRD

Function

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase

Protein Sequence

10 MPSQMEHAME 20 TMMFTFHKFA 30 GDKGYLTKED 40 LRVLMEKEFP 50 GFLENQKDPL 60 AVDKIMKDLD 70 QCRDGKVGFQ 80 SFFSLIAGLT 90 IACNDYFVVH MKQKGKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:1990665 AnxA2-p11 complex
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:0005576 extracellular region
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0001765 membrane raft assembly
Biological Process GO:0042789 mRNA transcription by RNA polymerase II
Biological Process GO:0045921 positive regulation of exocytosis
Biological Process GO:0051894 positive regulation of focal adhesion assembly
Biological Process GO:0043547 positive regulation of GTPase activity
Biological Process GO:1905686 positive regulation of plasma membrane repair
Biological Process GO:0010756 positive regulation of plasminogen activation
Biological Process GO:0051496 positive regulation of stress fiber assembly
Biological Process GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0072659 protein localization to plasma membrane
Biological Process GO:0050767 regulation of neurogenesis
Biological Process GO:0006900 vesicle budding from membrane

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] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.

[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.