Search Results

Overview

Uniprot IDP67870
Protein NameCasein kinase II subunit beta
Gene NameCSNK2B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
212 SNFKSPVKTIR****

Function

Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (PubMed:11239457, PubMed:16818610). Participates in Wnt signaling (By similarity)

Protein Sequence

10 MSSSEEVSWI 20 SWFCGLRGNE 30 FFCEVDEDYI 40 QDKFNLTGLN 50 EQVPHYRQAL 60 DMILDLEPDE 70 ELEDNPNQSD 80 LIEQAAEMLY 90 GLIHARYILT 100 NRGIAQMLEK 110 YQQGDFGYCP 120 RVYCENQPML 130 PIGLSDIPGE 140 AMVKLYCPKC 150 MDVYTPKSSR 160 HHHTDGAYFG 170 TGFPHMLFMV 180 HPEYRPKRPA 190 NQFVPRLYGF 200 KIHPMAYQLQ 210 LQAASNFKSP VKTIR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016605 PML body
Cellular Component GO:0005956 protein kinase CK2 complex
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0019887 protein kinase regulator activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0005102 signaling receptor binding
Biological Process GO:0033211 adiponectin-activated signaling pathway
Biological Process GO:0061154 endothelial tube morphogenesis
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0043537 negative regulation of blood vessel endothelial cell migration
Biological Process GO:0008285 negative regulation of cell population proliferation
Biological Process GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Process GO:1903901 negative regulation of viral life cycle
Biological Process GO:0032927 positive regulation of activin receptor signaling pathway
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0060391 positive regulation of SMAD protein signal transduction
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0007165 signal transduction
Biological Process GO:0075342 symbiont-mediated disruption of host cell PML body
Biological Process GO:0016055 Wnt signaling pathway

Reference

[1] 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.

[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] 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] 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.

[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.