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Overview

Uniprot IDQ13185
Protein NameChromobox protein homolog 3
Gene NameCBX3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 SNKTTLQKMGKKQNG
103 DSESDDSKSKKKRDA
106 SDDSKSKKKRDAADK
20 KKQNGKSKKVEEAEP
21 KQNGKSKKVEEAEPE
44 DRRVVNGKVEYFLKW
5 ***MASNKTTLQKMG
92 EKDGTKRKSLSDSES

Function

Component of heterochromatin, which recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression (PubMed:11242053). Also recognizes and binds histone H1.4 methylated at 'Lys-26' (H1.4K26me) (PubMed:16127177). Excluded from chromatin when histone H1.4 is Simultaneously methylated at Lys-26 (H1.4K26me) and phosphorylated at Ser-27 (H1.4S27Ph) (PubMed:16127177). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (PubMed:15502821). Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1 (By similarity). Mediates the recruitment of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (PubMed:28167679)

Protein Sequence

10 MASNKTTLQK 20 MGKKQNGKSK 30 KVEEAEPEEF 40 VVEKVLDRRV 50 VNGKVEYFLK 60 WKGFTDADNT 70 WEPEENLDCP 80 ELIEAFLNSQ 90 KAGKEKDGTK 100 RKSLSDSESD 110 DSKSKKKRDA 120 ADKPRGFARG 130 LDPERIIGAT 140 DSSGELMFLM 150 KWKDSDEADL 160 VLAKEANMKC 170 PQIVIAFYEE 180 RLTWHSCPED EAQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000775 chromosome, centromeric region
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0000779 condensed chromosome, centromeric region
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005637 nuclear inner membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005721 pericentric heterochromatin
Cellular Component GO:0090575 RNA polymerase II transcription regulator complex
Cellular Component GO:0035985 senescence-associated heterochromatin focus
Cellular Component GO:0090734 site of DNA damage
Cellular Component GO:0005819 spindle
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0160267 histone H1K26me1 reader activity
Molecular Function GO:0160268 histone H1K26me2 reader activity
Molecular Function GO:0062072 histone H3K9me2/3 reader activity
Molecular Function GO:1990226 histone methyltransferase binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0001221 transcription coregulator binding
Biological Process GO:0071549 cellular response to dexamethasone stimulus
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0048511 rhythmic process

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] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] 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.

[10] 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.

[11] 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.

[12] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[13] 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.