Search Results

Overview

Uniprot IDO15347
Protein NameHigh mobility group protein B3
Gene NameHMGB3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
161 EKDVADYKSKGKFDG
165 ADYKSKGKFDGAKGP
170 KGKFDGAKGPAKVAR
174 DGAKGPAKVARKKVE
76 VRYDREMKDYGPAKG
82 MKDYGPAKGGKKKKD
85 YGPAKGGKKKKDPNA

Function

Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity)

Protein Sequence

10 MAKGDPKKPK 20 GKMSAYAFFV 30 QTCREEHKKK 40 NPEVPVNFAE 50 FSKKCSERWK 60 TMSGKEKSKF 70 DEMAKADKVR 80 YDREMKDYGP 90 AKGGKKKKDP 100 NAPKRPPSGF 110 FLFCSEFRPK 120 IKSTNPGISI 130 GDVAKKLGEM 140 WNNLNDSEKQ 150 PYITKAAKLK 160 EKYEKDVADY 170 KSKGKFDGAK 180 GPAKVARKKV 190 EEEDEEEEEE 200 EEEEEEEEDE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0008301 DNA binding, bending
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0000400 four-way junction DNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0032392 DNA geometric change
Biological Process GO:0006310 DNA recombination
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045087 innate immune response

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[3] 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.

[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[5] 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.

[6] 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.