Search Results

Overview

Uniprot IDP45973
Protein NameChromobox protein homolog 5
Gene NameCBX5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
102 SNSADDIKSKKKREQ
125 ERGLEPEKIIGATDS
32 VLDRRVVKGQVEYLL
91 KSESNKRKSNFSNSA

Function

Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression (PubMed:40440427). In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph) (PubMed:19783980). 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). May contribute to the association of heterochromatin with the inner nuclear membrane by interactions with the lamin-B receptor (LBR) (PubMed:19783980). Involved in the formation of kinetochore through interaction with the MIS12 complex subunit NSL1 (PubMed:19783980, PubMed:20231385). Required for the formation of the inner centromere (PubMed:20231385)

Protein Sequence

10 MGKKTKRTAD 20 SSSSEDEEEY 30 VVEKVLDRRV 40 VKGQVEYLLK 50 WKGFSEEHNT 60 WEPEKNLDCP 70 ELISEFMKKY 80 KKMKEGENNK 90 PREKSESNKR 100 KSNFSNSADD 110 IKSKKKREQS 120 NDIARGFERG 130 LEPEKIIGAT 140 DSCGDLMFLM 150 KWKDTDEADL 160 VLAKEANVKC 170 PQIVIAFYEE 180 RLTWHAYPED 190 AENKEKETAK S

Gene Ontology

Classification GO ID Description
Cellular Component GO:0010369 chromocenter
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0000118 histone deacetylase complex
Cellular Component GO:0035097 histone methyltransferase complex
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005721 pericentric heterochromatin
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0090734 site of DNA damage
Cellular Component GO:0017053 transcription repressor complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0042826 histone deacetylase 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:0042802 identical protein binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0043021 ribonucleoprotein complex binding
Biological Process GO:0030261 chromosome condensation
Biological Process GO:0006974 DNA damage response
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0070828 heterochromatin organization
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0097355 protein localization to heterochromatin

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] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.