Search Results
Overview
| Uniprot ID | P12277 |
|---|---|
| Protein Name | Creatine kinase B-type |
| Gene Name | CKB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 11 | SNSHNALKLRFPAED |
| 156 | GERRAIEKLAVEALS |
| 242 | LRVISMQKGGNMKEV |
| 304 | IKLPNLGKHEKFSEV |
| 307 | PNLGKHEKFSEVLKR |
| 313 | EKFSEVLKRLRLQKR |
| 32 | AHNNHMAKVLTPELY |
Function
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0004111 | creatine kinase activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0140651 | futile creatine cycle |
| Biological Process | GO:0046314 | phosphocreatine biosynthetic process |
| Biological Process | GO:0021762 | substantia nigra development |
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] 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.