Search Results
Overview
| Uniprot ID | P63208 |
|---|---|
| Protein Name | S-phase kinase-associated protein 1 |
| Gene Name | SKP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 130 | VANMIKGKTPEEIRK |
| 142 | IRKTFNIKNDFTEEE |
| 155 | EEEAQVRKENQWCEE |
Function
Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2 (PubMed:25704143). SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2. Core component of the Cul7-RING(FBXW8) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35982156). Also acts as a core component of the Cul1-RING(FBXL4) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of BNIP3 and BNI3L (PubMed:36896912)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0031467 | Cul7-RING ubiquitin ligase complex |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0031519 | PcG protein complex |
| Cellular Component | GO:0019005 | SCF ubiquitin ligase complex |
| Molecular Function | GO:0008013 | beta-catenin binding |
| Molecular Function | GO:0097602 | cullin family protein binding |
| Molecular Function | GO:1990444 | F-box domain binding |
| Molecular Function | GO:0140677 | molecular function activator activity |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:1990757 | ubiquitin ligase activator activity |
| Molecular Function | GO:0160072 | ubiquitin ligase complex scaffold activity |
| Molecular Function | GO:1990756 | ubiquitin-like ligase-substrate adaptor activity |
| Biological Process | GO:0051298 | centrosome duplication |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0060271 | cilium assembly |
| Biological Process | GO:0000082 | G1/S transition of mitotic cell cycle |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0006879 | intracellular iron ion homeostasis |
| Biological Process | GO:0060173 | limb development |
| Biological Process | GO:0051457 | maintenance of protein location in nucleus |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0014033 | neural crest cell differentiation |
| Biological Process | GO:0043161 | proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0070936 | protein K48-linked ubiquitination |
| Biological Process | GO:0000209 | protein polyubiquitination |
| Biological Process | GO:0016567 | protein ubiquitination |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0030510 | regulation of BMP signaling pathway |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0010564 | regulation of cell cycle process |
| Biological Process | GO:0010824 | regulation of centrosome duplication |
| Biological Process | GO:0042752 | regulation of circadian rhythm |
| Biological Process | GO:2000001 | regulation of DNA damage checkpoint |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0050727 | regulation of inflammatory response |
| Biological Process | GO:1901524 | regulation of mitophagy |
| Biological Process | GO:0007346 | regulation of mitotic cell cycle |
| Biological Process | GO:0032006 | regulation of TOR signaling |
| Biological Process | GO:1904415 | regulation of xenophagy |
| Biological Process | GO:0031146 | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0051124 | synaptic assembly at neuromuscular junction |
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] 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.
[3] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.