Search Results

Overview

Uniprot IDQ9HB71
Protein NameCalcyclin-binding protein
Gene NameCACYBP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
19 EVKVLLEKATRKRVR
196 EGLMNVLKKIYEDGD
197 GLMNVLKKIYEDGDD
207 EDGDDDMKRTINKAW
212 DMKRTINKAWVESRE
223 ESREKQAKGDTEF**
33 RDALTAEKSKIETEI
35 ALTAEKSKIETEIKN
51 MQQKSQKKAELLDNE

Function

May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1)

Protein Sequence

10 MASEELQKDL 20 EEVKVLLEKA 30 TRKRVRDALT 40 AEKSKIETEI 50 KNKMQQKSQK 60 KAELLDNEKP 70 AAVVAPITTG 80 YTVKISNYGW 90 DQSDKFVKIY 100 ITLTGVHQVP 110 TENVQVHFTE 120 RSFDLLVKNL 130 NGKSYSMIVN 140 NLLKPISVEG 150 SSKKVKTDTV 160 LILCRKKVEN 170 TRWDYLTQVE 180 KECKEKEKPS 190 YDTETDPSEG 200 LMNVLKKIYE 210 DGDDDMKRTI 220 NKAWVESREK QAKGDTEF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030877 beta-catenin destruction complex
Cellular Component GO:0044297 cell body
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005641 nuclear envelope lumen
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0019005 SCF ubiquitin ligase complex
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0044548 S100 protein binding
Molecular Function GO:0015631 tubulin binding
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0055007 cardiac muscle cell differentiation
Biological Process GO:0071277 cellular response to calcium ion
Biological Process GO:0007507 heart development
Biological Process GO:0045740 positive regulation of DNA replication
Biological Process GO:0060416 response to growth hormone

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] 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] 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.

[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] 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.

[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.