Search Results
Overview
| Uniprot ID | Q6NZI2 |
|---|---|
| Protein Name | Caveolae-associated protein 1 |
| Gene Name | CAVIN1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | TTSNTVSKLLEKVRK |
| 122 | RKVSVNVKTVRGSLE |
| 137 | RQAGQIKKLEVNEAE |
| 165 | DEVKLPAKLSISKSL |
| 170 | PAKLSISKSLKESEA |
| 173 | LSISKSLKESEALPE |
| 233 | LRRVDDFKKAFSKEK |
| 299 | TSRDKLRKSFTPDHV |
| 312 | HVVYARSKTAVYKVP |
Function
Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005901 | caveola |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0045121 | membrane raft |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0042134 | rRNA primary transcript binding |
| Biological Process | GO:2000147 | positive regulation of cell motility |
| Biological Process | GO:0009306 | protein secretion |
| Biological Process | GO:0009303 | rRNA transcription |
| Biological Process | GO:0006363 | termination of RNA polymerase I transcription |
| Biological Process | GO:0006361 | transcription initiation at RNA polymerase I promoter |
Reference
[1] 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.
[2] 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.
[3] 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.